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Showing metabocard for Fe2+ (HMDB0000692)

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IdentificationTaxonomyOntologyPhysical propertiesSpectraBiological propertiesConcentrationsLinksReferencesenzymes (189)transporters (2) Show 191 proteinsXML
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Record Information
Version5.0
StatusDetected and Quantified
Creation Date2006-08-16 12:15:16 UTC
Update Date2022-03-07 02:49:05 UTC
HMDB IDHMDB0000692
Secondary Accession Numbers
  • HMDB00692
Metabolite Identification
Common NameFe2+
Description
Structure
Thumb
MOL3D MOLSDF3D SDFPDB3D PDBSMILESInChI

MOL for HMDB0000692 (Fe2+)

  Mrv1652309042000052D          

  1  0  0  0  0  0            999 V2000
   10.7983  -17.1792    0.0000 Fe  0  2  0  0  0  0  0  0  0  0  0  0
M  CHG  1   1   2
M  END
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3D MOL for HMDB0000692 (Fe2+)

HMDB0000692
     RDKit          3D
Fe2+
  1  0  0  0  0  0  0  0  0  0999 V2000
    0.0000    0.0000    0.0000 Fe  0  0  0  0  0 15  0  0  0  0  0  0
M  CHG  1   1   2
M  END
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3D SDF for HMDB0000692 (Fe2+)

  Mrv1652309042000052D          

  1  0  0  0  0  0            999 V2000
   10.7983  -17.1792    0.0000 Fe  0  2  0  0  0  0  0  0  0  0  0  0
M  CHG  1   1   2
M  END
> <DATABASE_ID>
HMDB0000692

> <DATABASE_NAME>
hmdb

> <SMILES>
[Fe++]

> <INCHI_IDENTIFIER>
InChI=1S/Fe/q+2

> <INCHI_KEY>
CWYNVVGOOAEACU-UHFFFAOYSA-N

> <FORMULA>
Fe

> <MOLECULAR_WEIGHT>
55.845

> <EXACT_MASS>
55.934942133

> <JCHEM_ACCEPTOR_COUNT>
0

> <JCHEM_ATOM_COUNT>
1

> <JCHEM_AVERAGE_POLARIZABILITY>
1.7784

> <JCHEM_BIOAVAILABILITY>
1

> <JCHEM_DONOR_COUNT>
0

> <JCHEM_FORMAL_CHARGE>
2

> <JCHEM_GHOSE_FILTER>
0

> <JCHEM_IUPAC>
lambda2-iron(2+) ion

> <JCHEM_LOGP>
-0.77

> <JCHEM_MDDR_LIKE_RULE>
0

> <JCHEM_NUMBER_OF_RINGS>
0

> <JCHEM_PHYSIOLOGICAL_CHARGE>
2

> <JCHEM_PKA>
5.46

> <JCHEM_PKA_STRONGEST_ACIDIC>
4.58

> <JCHEM_POLAR_SURFACE_AREA>
0.0

> <JCHEM_REFRACTIVITY>
0.0

> <JCHEM_ROTATABLE_BOND_COUNT>
0

> <JCHEM_RULE_OF_FIVE>
1

> <JCHEM_TRADITIONAL_IUPAC>
lambda2-iron(2+) ion

> <JCHEM_VEBER_RULE>
1

$$$$
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3D-SDF for HMDB0000692 (Fe2+)

HMDB0000692
     RDKit          3D
Fe2+
  1  0  0  0  0  0  0  0  0  0999 V2000
    0.0000    0.0000    0.0000 Fe  0  0  0  0  0 15  0  0  0  0  0  0
M  CHG  1   1   2
M  END
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PDB for HMDB0000692 (Fe2+)

HEADER    PROTEIN                                 04-SEP-20   NONE
TITLE     NULL                                                        
COMPND    NULL                                                        
SOURCE    NULL                                                        
KEYWDS    NULL                                                        
EXPDTA    NULL                                                        
AUTHOR    Marvin                                                      
REVDAT   1   04-SEP-20         0                                  
HETATM    1 Fe   UNK     0      20.157 -32.068   0.000  0.00  0.00          Fe+2
MASTER        0    0    0    0    0    0    0    0    1    0    0    0
END
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3D PDB for HMDB0000692 (Fe2+)

COMPND    HMDB0000692
HETATM    1 FE1  UNL     1       0.000   0.000   0.000  1.00  0.00          FE2+
END
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SMILES for HMDB0000692 (Fe2+)

[Fe++]
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INCHI for HMDB0000692 (Fe2+)

InChI=1S/Fe/q+2
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View in JSmolView Stereo Labels
Synonyms
Chemical FormulaFe
Average Molecular Weight55.845
Monoisotopic Molecular Weight55.934942133
IUPAC Namelambda2-iron(2+) ion
Traditional Namelambda2-iron(2+) ion
CAS Registry Number15438-31-0
SMILES
[Fe++]
InChI Identifier
InChI=1S/Fe/q+2
InChI KeyCWYNVVGOOAEACU-UHFFFAOYSA-N
Chemical Taxonomy
Description Belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Ontology
Physiological effect
Health effect
Disposition
Biological locationRoute of exposureSource
Process
Naturally occurring process
Role
Industrial applicationBiological role
Physical Properties
StateSolid
Experimental Molecular Properties
PropertyValueReference
Melting Point1538 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Experimental Chromatographic PropertiesNot Available
Predicted Molecular Properties
PropertyValueSource
logP-0.77ChemAxon
pKa (Strongest Acidic)4.58ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Predicted Chromatographic Properties

Predicted Kovats Retention Indices

Underivatized

MetaboliteSMILESKovats RI ValueColumn TypeReference
Fe2+[Fe++]701.9Standard polar33892256
Fe2+[Fe++]271.5Standard non polar33892256
Fe2+[Fe++]55.1Semi standard non polar33892256
Spectra

MS/MS Spectra

Spectrum TypeDescriptionSplash KeyDeposition DateSourceView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 10V, Positive-QTOFsplash10-0a4i-9000000000-af3e7aec4f5bd96686832016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 20V, Positive-QTOFsplash10-0a4i-9000000000-af3e7aec4f5bd96686832016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 40V, Positive-QTOFsplash10-0a4i-9000000000-af3e7aec4f5bd96686832016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 10V, Negative-QTOFsplash10-0udi-9000000000-3335fec4c3184739b75e2016-08-03Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 20V, Negative-QTOFsplash10-0udi-9000000000-3335fec4c3184739b75e2016-08-03Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Fe2+ 40V, Negative-QTOFsplash10-0udi-9000000000-3335fec4c3184739b75e2016-08-03Wishart LabView Spectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
Biospecimen Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Locations
  • Brain
  • Liver
Pathways
Normal Concentrations
Abnormal Concentrations
Associated Disorders and Diseases
Disease References
Multiple sclerosis
  1. Forte G, Visconti A, Santucci S, Ghazaryan A, Figa-Talamanca L, Cannoni S, Bocca B, Pino A, Violante N, Alimonti A, Salvetti M, Ristori G: Quantification of chemical elements in blood of patients affected by multiple sclerosis. Ann Ist Super Sanita. 2005;41(2):213-6. [PubMed:16244395 ]
Parkinson's disease
  1. Forte G, Alimonti A, Pino A, Stanzione P, Brescianini S, Brusa L, Sancesario G, Violante N, Bocca B: Metals and oxidative stress in patients with Parkinson's disease. Ann Ist Super Sanita. 2005;41(2):189-95. [PubMed:16244392 ]
Alzheimer's disease
  1. Molina JA, Jimenez-Jimenez FJ, Aguilar MV, Meseguer I, Mateos-Vega CJ, Gonzalez-Munoz MJ, de Bustos F, Porta J, Orti-Pareja M, Zurdo M, Barrios E, Martinez-Para MC: Cerebrospinal fluid levels of transition metals in patients with Alzheimer's disease. J Neural Transm (Vienna). 1998;105(4-5):479-88. [PubMed:9720975 ]
  2. Bocca B, Forte G, Petrucci F, Pino A, Marchione F, Bomboi G, Senofonte O, Giubilei F, Alimonti A: Monitoring of chemical elements and oxidative damage in patients affected by Alzheimer's disease. Ann Ist Super Sanita. 2005;41(2):197-203. [PubMed:16244393 ]
Fibromyalgia
  1. Ortancil O, Sanli A, Eryuksel R, Basaran A, Ankarali H: Association between serum ferritin level and fibromyalgia syndrome. Eur J Clin Nutr. 2010 Mar;64(3):308-12. doi: 10.1038/ejcn.2009.149. Epub 2010 Jan 20. [PubMed:20087382 ]
Iron deficiency
  1. Canatan D, Akdeniz SK: Iron and ferritin levels in saliva of patients with thalassemia and iron deficiency anemia. Mediterr J Hematol Infect Dis. 2012;4(1):e2012051. doi: 10.4084/MJHID.2012.051. Epub 2012 Aug 9. [PubMed:22973495 ]
  2. Mishra OP, Agarwal KN, Agarwal RM: Salivary iron status in children with iron deficiency and iron overload. J Trop Pediatr. 1992 Apr;38(2):64-7. [PubMed:1569637 ]
Associated OMIM IDs
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB030855
KNApSAcK IDNot Available
Chemspider ID25394
KEGG Compound IDC14818
BioCyc IDFE%2b2
BiGG ID33552
Wikipedia LinkIron
METLIN IDNot Available
PubChem Compound27284
PDB IDFE2
ChEBI ID29033
Food Biomarker OntologyNot Available
VMH IDNot Available
MarkerDB IDMDB00000221
Good Scents IDNot Available
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References

Only showing the first 10 proteins. There are 191 proteins in total.

Show all enzymes and transporters

Enzymes

Enzyme Details
1. 5-aminolevulinate synthase, erythroid-specific, mitochondrial
General function:
Involved in 5-aminolevulinate synthase activity
Specific function:
Not Available
Gene Name:
ALAS2
Uniprot ID:
P22557
Molecular weight:
64632.86
Enzyme Details
2. 85/88 kDa calcium-independent phospholipase A2
General function:
Involved in metabolic process
Specific function:
Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.
Gene Name:
PLA2G6
Uniprot ID:
O60733
Molecular weight:
84092.635
Enzyme Details
3. Tartrate-resistant acid phosphatase type 5
General function:
Involved in hydrolase activity
Specific function:
Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias.
Gene Name:
ACP5
Uniprot ID:
P13686
Molecular weight:
36598.47
Enzyme Details
4. Ribonucleoside-diphosphate reductase large subunit
General function:
Involved in oxidation reduction
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Gene Name:
RRM1
Uniprot ID:
P23921
Molecular weight:
90069.375
Enzyme Details
5. Ribonucleoside-diphosphate reductase subunit M2
General function:
Involved in oxidoreductase activity
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.
Gene Name:
RRM2
Uniprot ID:
P31350
Molecular weight:
44877.25
Enzyme Details
6. NADH-ubiquinone oxidoreductase chain 1
General function:
Involved in oxidation reduction
Specific function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:
MT-ND1
Uniprot ID:
P03886
Molecular weight:
35660.055
Enzyme Details
7. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
General function:
Involved in NADH dehydrogenase activity
Specific function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
Gene Name:
NDUFB1
Uniprot ID:
O75438
Molecular weight:
6961.2
Enzyme Details
8. NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:
NDUFS2
Uniprot ID:
O75306
Molecular weight:
51851.59
Enzyme Details
9. Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
General function:
Involved in succinate dehydrogenase activity
Specific function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHC
Uniprot ID:
Q99643
Molecular weight:
16650.185
Enzyme Details
10. Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
General function:
Amino acid transport and metabolism
Specific function:
Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.
Gene Name:
PAOX
Uniprot ID:
Q6QHF9
Molecular weight:
55512.64

Transporters

Enzyme Details
1. Cubilin
General function:
Involved in calcium ion binding
Specific function:
Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands required calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface
Gene Name:
CUBN
Uniprot ID:
O60494
Molecular weight:
398672.8
Enzyme Details
2. Proton-coupled folate transporter
General function:
Involved in transmembrane transport
Specific function:
Has been shown to act both as an intestinal proton- coupled high-affinity folate transporter and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. The iron is then released from heme and may be transported into the bloodstream. Dietary heme iron is an important nutritional source of iron. Shows a higher affinity for folate than heme
Gene Name:
SLC46A1
Uniprot ID:
Q96NT5
Molecular weight:
49770.0

Only showing the first 10 proteins. There are 191 proteins in total.

Show all enzymes and transporters