Identification |
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Name: | Xanthine dehydrogenase molybdenum-binding subunit |
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Synonyms: | Not Available |
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Gene Name: | xdhA |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in oxidoreductase activity |
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Specific Function: | Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). Deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage |
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Cellular Location: | Not Available |
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SMPDB Pathways: | - adenosine nucleotides degradation PW002091
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KEGG Pathways: | |
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KEGG Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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catalytic activity | oxidoreductase activity | Process |
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metabolic process | oxidation reduction |
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Gene Properties |
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Blattner: | b2866 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 64.62 |
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Left Sequence End | 2998367 |
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Right Sequence End | 3000625 |
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Gene Sequence: | >2259 bp
ATGCGCGTCGATGCCATTGCTAAGGTCACCGGGCGGGCACGATATACTGACGATTATGTT
ATGGCGGGCATGTGTTATGCGAAATATGTACGTAGCCCTATCGCACATGGTTATGCCGTA
AGTATTAATGATGAACAAGCCAGAAGTTTGCCGGGCGTACTGGCGATTTTTACCTGGGAA
GATGTGCCTGATATTCCATTCGCTACAGCTGGGCATGCCTGGACACTTGACGAAAACAAG
CGCGATACCGCCGATCGCGCACTGCTAACTCGCCATGTTCGTCATCATGGTGACGCCGTT
GCCATCGTCGTGGCCCGCGATGAACTCACGGCAGAAAAAGCGGCGCAATTGGTCAGCATT
GAGTGGCAAGAATTACCCGTTATCACCACGCCAGAAGCGGCGCTGGCAGAAGACGCTGCA
CCAATCCATAACGGTGGCAATTTACTGAAACAAAGCACGATGTCGACGGGTAATGTCCAA
CAAACAATCGATGCCGCCGACTACCAGGTACAGGGGCACTATCAGACCCCCGTTATTCAA
CATTGTCACATGGAAAGCGTAACATCGCTGGCGTGGATGGAGGATGACTCGCGAATTACC
ATCGTTTCCAGCACCCAGATCCCGCACATTGTTCGCCGCGTGGTTGGTCAGGCGCTGGAT
ATTCCCTGGTCATGCGTACGAGTCATCAAACCATTTGTCGGTGGCGGTTTTGGTAATAAA
CAGGATGTACTGGAAGAGCCAATGGCGGCATTCCTGACCAGCAAGCTTGGCGGCATTCCG
GTGAAAGTTTCCCTTAGCCGTGAAGAGTGTTTCCTCGCAACCCGTACCCGCCACGCTTTT
ACCATTGACGGGCAAATGGGCGTGAACCGCGACGGAACATTGAAAGGTTATAGTCTGGAT
GTTCTGTCTAACACCGGCGCTTATGCATCTCACGGGCACTCCATCGCTTCTGCGGGGGGG
AATAAAGTCGCTTACCTTTATCCTCGTTGTGCCTACGCTTACAGTTCAAAGACCTGCTAT
ACCAACCTCCCCTCGGCTGGTGCGATGCGTGGTTATGGCGCGCCACAAGTCGTATTTGCC
GTTGAGTCTATGCTTGATGACGCCGCGACAGCGTTAGGTATTGATCCTGTTGAAATTCGT
TTACGCAACGCCGCCCGCGAAGGAGATGCTAATCCGCTCACGGGCAAACGTATTTACAGC
GCAGGGTTGCCGGAGTGTCTTGAAAAAGGCCGGAAAATCTTTGAATGGGAAAAACGCCGT
GCAGAATGCCAGAACCAGCAAGGCAATTTGCGCCGCGGCGTTGGCGTCGCCTGTTTTAGC
TACACCTCTAACACCTGGCCTGTCGGCGTAGAAATAGCAGGCGCGCGCCTTCTGATGAAT
CAGGATGGAACCATCAACGTGCAAAGCGGCGCGACGGAAATCGGTCAGGGTGCCGACACC
GTCTTCTCGCAAATGGTGGCAGAAACCGTGGGGGTTCCGGTCAGCGACGTTCGCGTTATT
TCAACTCAAGATACCGACGTTACGCCGTTCGATCCCGGCGCATTTGCCTCACGCCAGAGC
TATGTTGCCGCGCCTGCGCTGCGCAGTGCGGCACTATTATTAAAAGAGAAAATCATCGCT
CACGCCGCAGTCATGCTACATCAGTCAGCGATGAATCTGACCCTGATAAAAGGCCATATC
GTGCTGGTTGAACGACCGGAAGAGCCGTTAATGTCGTTAAAAGATTTGGCGATGGACGCT
TTCTACCACCCTGAACGCGGCGGGCAGCTCTCTGCTGAAAGCTCCATCAAAACCACCACT
AACCCACCGGCGTTTGGCTGTACCTTTGTTGATCTGACGGTCGATATTGCGCTGTGCAAA
GTCACCATCAACCGCATCCTCAACGTTCATGATTCAGGGCATATTCTTAATCCACTGCTG
GCAGAAGGTCAGGTACACGGCGGAATGGGAATGGGCATTGGCTGGGCGCTATTTGAAGAG
ATGATCATCGATGCTAAAAGCGGCGTGGTCCGTAACCCCAATCTGCTGGATTACAAAATG
CCGACCATGCCGGATCTGCCACAACTGGAAAGCGCGTTCGTCGAAATCAATGAGCCGCAA
TCCGCATACGGACATAAGTCACTGGGTGAGCCACCAATAATTCCTGTTGCCGCTGCTATT
CGTAACGCGGTGAAGATGGCTACCGGTGTTGCAATCAATACACTGCCGCTGACGCCAAAA
CGGTTATATGAAGAGTTCCATCTGGCAGGATTGATTTGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 752 |
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Protein Molecular Weight: | 81320 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Xanthine dehydrogenase molybdenum-binding subunit
MRVDAIAKVTGRARYTDDYVMAGMCYAKYVRSPIAHGYAVSINDEQARSLPGVLAIFTWE
DVPDIPFATAGHAWTLDENKRDTADRALLTRHVRHHGDAVAIVVARDELTAEKAAQLVSI
EWQELPVITTPEAALAEDAAPIHNGGNLLKQSTMSTGNVQQTIDAADYQVQGHYQTPVIQ
HCHMESVTSLAWMEDDSRITIVSSTQIPHIVRRVVGQALDIPWSCVRVIKPFVGGGFGNK
QDVLEEPMAAFLTSKLGGIPVKVSLSREECFLATRTRHAFTIDGQMGVNRDGTLKGYSLD
VLSNTGAYASHGHSIASAGGNKVAYLYPRCAYAYSSKTCYTNLPSAGAMRGYGAPQVVFA
VESMLDDAATALGIDPVEIRLRNAAREGDANPLTGKRIYSAGLPECLEKGRKIFEWEKRR
AECQNQQGNLRRGVGVACFSYTSNTWPVGVEIAGARLLMNQDGTINVQSGATEIGQGADT
VFSQMVAETVGVPVSDVRVISTQDTDVTPFDPGAFASRQSYVAAPALRSAALLLKEKIIA
HAAVMLHQSAMNLTLIKGHIVLVERPEEPLMSLKDLAMDAFYHPERGGQLSAESSIKTTT
NPPAFGCTFVDLTVDIALCKVTINRILNVHDSGHILNPLLAEGQVHGGMGMGIGWALFEE
MIIDAKSGVVRNPNLLDYKMPTMPDLPQLESAFVEINEPQSAYGHKSLGEPPIIPVAAAI
RNAVKMATGVAINTLPLTPKRLYEEFHLAGLI |
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References |
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External Links: | |
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General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Xi, H., Schneider, B. L., Reitzer, L. (2000). "Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage." J Bacteriol 182:5332-5341. Pubmed: 10986234
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