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Showing Protein Aflatoxin B1 aldehyde reductase member 2 (HMDBP03221)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 9 metabolites
Identification
HMDB Protein ID HMDBP03221
Secondary Accession Numbers
  • 8786
Name Aflatoxin B1 aldehyde reductase member 2
Synonyms
  1. AFB1 aldehyde reductase 1
  2. AFB1-AR 1
  3. Aldoketoreductase 7
  4. SSA reductase
  5. Succinic semialdehyde reductase
Gene Name AKR7A2
Protein Type Enzyme
Biological Properties
General Function Energy production and conversion
Specific Function Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.
Pathways
  • Metabolism of xenobiotics by cytochrome P450
Reactions
4-Hydroxybutyric acid + NADP → Succinic acid semialdehyde + NADPH details
GO Classification
Biological Process
cellular aldehyde metabolic process
daunorubicin metabolic process
doxorubicin metabolic process
carbohydrate metabolic process
Cellular Component
Golgi apparatus
Function
catalytic activity
oxidoreductase activity
Molecular Function
electron carrier activity
alditol:NADP+ 1-oxidoreductase activity
phenanthrene-9,10-epoxide hydrolase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
  2. Golgi apparatus
Gene Properties
Chromosome Location 1
Locus 1p36.13
SNPs AKR7A2
Gene Sequence 
>1080 bp
ATGCTGAGTGCCGCGTCTCGCGTAGTCTCCCGCGCCGCCGTCCACTGCGCGCTTCGCTCT
CCGCCGCCCGAGGCCCGCGCGCTCGCCATGTCCCGGCCACCGCCACCGCGGGTCGCCTCG
GTGCTGGGCACCATGGAGATGGGGCGCCGCATGGACGCGCCCGCCAGCGCCGCGGCCGTG
CGCGCCTTTCTGGAGCGCGGCCACACCGAACTGGACACGGCCTTCATGTACAGCGACGGC
CAGTCCGAGACCATCCTGGGCGGCCTGGGGCTCGGGCTGGGCGGTGGCGACTGCAGAGTG
AAAATTGCCACCAAGGCCAACCCTTGGGATGGAAAATCACTAAAGCCTGACAGTGTCCGG
TCCCAGCTGGAGACGTCATTGAAGAGGCTGCAGTGTCCCCAAGTGGACCTCTTCTACCTA
CACGCACCTGACCACGGCACCCCGGTGGAAGAGACGCTGCATGCCTGCCAGCGGCTGCAC
CAGGAGGGCAAGTTCGTGGAGCTTGGCCTCTCCAACTATGCTAGCTGGGAAGTGGCCGAG
ATCTGTACCCTCTGCAAGAGCAATGGCTGGATCCTGCCCACTGTGTACCAGGGCATGTAC
AACGCCACCACCCGGCAGGTGGAAACGGAGCTCTTCCCCTGCCTCAGGCACTTTGGACTG
AGGTTCTATGCCTACAACCCTCTGGCTGGGGGCCTGCTGACTGGCAAGTACAAGTATGAG
GACAAGGACGGGAAACAGCCTGTGGGCCGCTTCTTTGGGAATAGCTGGGCTGAGACCTAC
AGGAATCGCTTCTGGAAGGAGCACCACTTCGAGGCCATTGCGTTGGTGGAGAAGGCCCTG
CAGGCCGCATATGGCGCCAGCGCCCCCAGTGTGACCTCGGCTGCCCTCCGGTGGATGTAC
CACCACTCACAGCTGCAGGGTGCCCACGGGGACGCGGTCATCCTGGGCATGTCCAGCCTG
GAGCAGCTGGAGCAGAACTTGGCAGCAACAGAGGAAGGGCCCCTGGAGCCGGCTGTCGTG
GATGCCTTTAATCAAGCCTGGCATTTGGTTGCTCACGAATGTCCCAACTACTTCCGCTAG
Protein Properties
Number of Residues 359
Molecular Weight 39588.65
Theoretical pI 7.171
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Aflatoxin B1 aldehyde reductase member 2
MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRVASVLGTMEMGRRMDAPASAAAV
RAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGKSLKPDSVR
SQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAE
ICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYE
DKDGKQPVGRFFGNSWAETYRNRFWKEHHFEAIALVEKALQAAYGASAPSVTSAALRWMY
HHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAWHLVAHECPNYFR
GenBank ID Protein 41327764
UniProtKB/Swiss-Prot ID O43488
UniProtKB/Swiss-Prot Entry Name ARK72_HUMAN
PDB IDs
GenBank Gene ID NM_003689.2
GeneCard ID AKR7A2
GenAtlas ID Not Available
HGNC ID HGNC:389
References
General References
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  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. O'connor T, Ireland LS, Harrison DJ, Hayes JD: Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members. Biochem J. 1999 Oct 15;343 Pt 2:487-504. [PubMed:10510318 ]
  5. Ireland LS, Harrison DJ, Neal GE, Hayes JD: Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase. Biochem J. 1998 May 15;332 ( Pt 1):21-34. [PubMed:9576847 ]
  6. Praml C, Savelyeva L, Perri P, Schwab M: Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a region frequently altered in human tumor cells. Cancer Res. 1998 Nov 15;58(22):5014-8. [PubMed:9823300 ]
  7. Kelly VP, Sherratt PJ, Crouch DH, Hayes JD: Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins. Biochem J. 2002 Sep 15;366(Pt 3):847-61. [PubMed:12071861 ]
  8. Lyon RC, Johnston SM, Watson DG, McGarvie G, Ellis EM: Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2. J Biol Chem. 2007 Sep 7;282(36):25986-92. Epub 2007 Jun 25. [PubMed:17591773 ]
  9. Praml C, Schulz W, Claas A, Mollenhauer J, Poustka A, Ackermann R, Schwab M, Henrich KO: Genetic variation of Aflatoxin B1 aldehyde reductase genes (AFAR) in human tumour cells. Cancer Lett. 2008 Dec 8;272(1):160-6. doi: 10.1016/j.canlet.2008.07.013. Epub 2008 Aug 26. [PubMed:18752886 ]