Aldehyde oxidoreductase

Name	Aldehyde oxidoreductase
Synonyms	1.2.99.7 Molybdenum iron sulfur protein
Gene Name	mop
Organism	Desulfovibrio gigas
Amino acid sequence	>lcl\|BSEQ0020527\|Aldehyde oxidoreductase MIQKVITVNGIEQNLFVDAEALLSDVLRQQLGLTGVKVGCEQGQCGACSVILDGKVVRAC VTKMKRVADGAQITTIEGVGQPENLHPLQKAWVLHGGAQCGFCSPGFIVSAKGLLDTNAD PSREDVRDWFQKHRNACRCTGYKPLVDAVMDAAAVINGKKPETDLEFKMPADGRIWGSKY PRPTAVAKVTGTLDYGADLGLKMPAGTLHLAMVQAKVSHANIKGIDTSEALTMPGVHSVI THKDVKGKNRITGLITFPTNKGDGWDRPILCDEKVFQYGDCIALVCADSEANARAAAEKV KVDLEELPAYMSGPAAAAEDAIEIHPGTPNVYFEQPIVKGEDTGPIFASADVTVEGDFYV GRQPHMPIEPDVAFAYMGDDGKCYIHSKSIGVHLHLYMIAPGVGLEPDQLVLVANPMGGT FGYKFSPTSEALVAVAAMATGRPVHLRYNYQQQQQYTGKRSPWEMNVKFAAKKDGTLLAM ESDWLVDHGPYSEFGDLLTLRGAQFIGAGYNIPNIRGLGRTVATNHVWGSAFRGYGAPQS MFASECLMDMLAEKLGMDPLELRYKNAYRPGDTNPTGQEPEVFSLPDMIDQLRPKYQAAL EKAQKESTATHKKGVGISIGVYGSGLDGPDASEAWAELNADGTITVHTAWEDHGQGADIG CVGTAHEALRPMGVAPEKIKFTWPNTATTPNSGPSGGSRQQVMTGNAIRVACENLLKACE KPGGGYYTYDELKAADKPTKITGNWTASGATHCDAVTGLGKPFVVYMYGVFMAEVTVDVA TGQTTVDGMTLMADLGSLCNQLATDGQIYGGLAQGIGLALSEDFEDIKKHATLVGAGFPF IKQIPDKLDIVYVNHPRPDGPFGASGVGELPLTSPHAAIINAIKSATGVRIYRLPAYPEK VLEALKA
Number of residues	None
Molecular Weight	97033.97
Theoretical pI	5.95
GO Classification	Functions metal ion binding electron carrier activity 2 iron, 2 sulfur cluster binding aldehyde dehydrogenase (FAD-independent) activity Processes Components
General Function	Metal ion binding
Specific Function	None
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	Q46509
UniProtKB Entry Name
Cellular Location	None
Gene sequence	>lcl\|BSEQ0002893\|2724 bp ATGATTCAAAAAGTAATCACCGTCAACGGCATCGAGCAGAATCTGTTCGTGGACGCCGAA GCCCTGCTGTCTGACGTGCTGCGTCAGCAACTCGGGCTCACCGGCGTCAAGGTGGGCTGC GAACAGGGCCAGTGCGGCGCCTGCTCCGTCATCCTGGATGGCAAAGTGGTGCGCGCCTGC GTCACCAAAATGAAGCGCGTGGCCGACGGCGCGCAGATCACCACCATCGAAGGCGTGGGC CAGCCGGAGAACCTGCATCCGTTGCAGAAAGCCTGGGTGCTGCACGGCGGCGCGCAATGC GGCTTCTGCTCCCCCGGCTTCATCGTCTCCGCCAAGGGCCTCCTGGACACCAACGCCGAC CCCTCTCGCGAAGACGTGCGTGATTGGTTCCAGAAGCATCGCAATGCTTGCCGTTGCACC GGCTACAAGCCGCTGGTGGACGCCGTGATGGACGCCGCCGCGGTCATCAATGGCAAGAAG CCCGAAACCGACCTGGAATTCAAGATGCCCGCCGACGGCCGCATCTGGGGCTCCAAATAC CCCCGCCCCACGGCCGTGGCCAAGGTCACCGGCACGCTGGACTACGGCGCGGACCTGGGC CTGAAAATGCCCGCTGGCACCCTGCACTTGGCCATGGTCCAGGCCAAGGTGTCCCACGCC AACATCAAGGGCATCGACACCTCCGAAGCCCTCACCATGCCCGGCGTCCACAGCGTCATC ACGCACAAGGACGTCAAGGGCAAGAACCGCATCACCGGCCTCATCACCTTCCCCACCAAC AAGGGTGACGGCTGGGATCGTCCCATCCTGTGCGACGAAAAGGTCTTCCAGTACGGCGAC TGCATCGCCCTGGTCTGCGCCGACTCCGAAGCCAACGCCCGCGCCGCGGCCGAAAAGGTG AAGGTGGACCTGGAAGAACTGCCCGCGTACATGAGCGGCCCTGCCGCTGCGGCCGAGGAT GCCATTGAGATCCATCCCGGCACGCCCAACGTGTACTTTGAACAGCCCATCGTCAAGGGC GAAGACACCGGCCCCATCTTCGCCTCGGCCGACGTCACCGTGGAAGGCGACTTCTACGTG GGCCGCCAGCCGCACATGCCCATCGAACCAGACGTAGCCTTTGCCTACATGGGCGACGAC GGCAAGTGCTACATCCACTCCAAGTCCATCGGCGTGCACCTGCACCTGTACATGATCGCC CCCGGCGTGGGCCTGGAACCCGATCAGCTGGTGCTGGTGGCCAACCCCATGGGCGGCACC TTCGGCTACAAGTTCAGCCCCACCTCCGAAGCCCTGGTGGCCGTGGCGGCCATGGCCACG GGCCGCCCCGTGCACCTGCGCTACAACTATCAGCAGCAGCAGCAGTACACCGGCAAGCGC TCCCCGTGGGAAATGAACGTCAAGTTCGCGGCCAAGAAAGACGGCACGCTCCTGGCCATG GAATCCGACTGGCTGGTGGACCACGGCCCCTACTCGGAATTCGGCGACCTCCTGACCCTG CGCGGCGCACAGTTCATCGGCGCCGGCTACAACATCCCCAACATCCGCGGCCTCGGTCGC ACTGTGGCCACCAACCACGTCTGGGGCTCTGCCTTCCGCGGCTACGGTGCGCCTCAGTCC ATGTTCGCCTCCGAATGTCTCATGGACATGCTGGCGGAAAAGCTGGGCATGGACCCGCTG GAACTGCGCTACAAGAACGCCTACCGCCCCGGCGACACCAACCCCACCGGCCAGGAACCT GAAGTCTTCAGCCTGCCGGACATGATCGACCAGCTGCGGCCCAAGTATCAGGCTGCTCTG GAAAAGGCCCAAAAGGAATCCACCGCCACCCATAAGAAGGGCGTGGGCATCTCCATCGGC GTGTACGGCAGCGGCCTGGACGGCCCTGACGCCTCCGAAGCCTGGGCCGAGCTCAATGCC GACGGCACCATCACCGTGCATACGGCCTGGGAAGACCATGGCCAGGGCGCGGACATCGGC TGCGTGGGCACGGCGCACGAAGCCCTGCGTCCCATGGGCGTGGCTCCGGAAAAGATCAAG TTCACCTGGCCCAACACCGCCACCACCCCCAACTCCGGCCCCTCCGGAGGCTCCCGCCAG CAGGTGATGACCGGCAACGCCATCCGCGTGGCCTGTGAAAACCTCCTCAAGGCCTGTGAA AAGCCCGGCGGCGGCTACTACACCTACGACGAACTGAAAGCCGCGGACAAGCCCACCAAG ATCACCGGCAACTGGACCGCCAGCGGGGCCACCCACTGCGACGCCGTGACCGGCCTTGGC AAGCCCTTTGTGGTGTACATGTACGGCGTGTTCATGGCCGAAGTGACCGTGGACGTGGCC ACCGGCCAGACCACCGTGGACGGCATGACCCTCATGGCCGACCTCGGCAGCCTCTGCAAC CAGCTGGCCACCGACGGGCAGATCTACGGCGGCCTGGCCCAGGGCATCGGCCTGGCCCTG TCCGAGGACTTCGAGGACATCAAGAAGCACGCCACCCTCGTGGGCGCGGGCTTCCCGTTC ATCAAGCAGATCCCGGACAAGCTGGACATCGTGTACGTGAACCATCCGCGTCCGGACGGC CCCTTCGGCGCTTCCGGTGTGGGCGAACTGCCCCTGACCAGCCCGCACGCGGCCATCATC AACGCCATCAAGAGCGCCACTGGCGTGCGCATCTACCGCCTCCCGGCCTACCCGGAAAAG GTGCTGGAAGCCTTGAAGGCCTAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Thoenes U, Flores OL, Neves A, Devreese B, Van Beeumen JJ, Huber R, Romao MJ, LeGall J, Moura JJ, Rodrigues-Pousada C: Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase. Eur J Biochem. 1994 Mar 15;220(3):901-10. [8143744 ] Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R: Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science. 1995 Nov 17;270(5239):1170-6. [7502041 ] Huber R, Hof P, Duarte RO, Moura JJ, Moura I, Liu MY, LeGall J, Hille R, Archer M, Romao MJ: A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes. Proc Natl Acad Sci U S A. 1996 Aug 20;93(17):8846-51. [8799115 ] Rebelo JM, Dias JM, Huber R, Moura JJ, Romao MJ: Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A. J Biol Inorg Chem. 2001 Oct;6(8):791-800. [11713686 ]

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