| Identification |
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| Name: | Hydrogenase-2 small chain |
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| Synonyms: | - HYD2
- Membrane-bound hydrogenase 2 small subunit
- NiFe hydrogenase
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| Gene Name: | hybO |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in NADH dehydrogenase (ubiquinone) activity |
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| Specific Function: | This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake |
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| Cellular Location: | Cell membrane; Peripheral membrane protein; Periplasmic side. Periplasm |
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| SMPDB Pathways: | Not Available |
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| KEGG Pathways: | - Microbial metabolism in diverse environments ec01120
- Trinitrotoluene degradation ec00633
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| KEGG Reactions: | |
1.02,4-Diamino-6-nitrotoluene | ↔ | 1.02,4-Diamino-6-hydroxylaminotoluene |
| 1.02,4-Diamino-6-nitrotoluene ↔ 1.02,4-Diamino-6-hydroxylaminotoluene ReactionCard | |
1.0 | + | 1.0Acceptor | ↔ | 1.0Reduced acceptor |
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| Complex Reactions: | | | | | |
2.0 | + | 1.0 | + | 1.0Menaquinone 8 | → | 1.0 | + | 2.0 |
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| Metabolites: | |
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| GO Classification: | | Component |
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| ferredoxin hydrogenase complex | | macromolecular complex | | protein complex | | Function |
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| 4 iron, 4 sulfur cluster binding | | binding | | catalytic activity | | cofactor binding | | ferredoxin hydrogenase activity | | iron-sulfur cluster binding | | metal cluster binding | | NADH dehydrogenase (quinone) activity | | NADH dehydrogenase (ubiquinone) activity | | NADH dehydrogenase activity | | oxidoreductase activity | | oxidoreductase activity, acting on hydrogen as donor | | oxidoreductase activity, acting on hydrogen as donor, iron-sulfur protein as acceptor | | oxidoreductase activity, acting on NADH or NADPH | | quinone binding | | Process |
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| metabolic process | | oxidation reduction |
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| Gene Properties |
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| Blattner: | b2997 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 67.75 |
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| Left Sequence End | 3143165 |
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| Right Sequence End | 3144283 |
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| Gene Sequence: | >1119 bp
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 372 |
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| Protein Molecular Weight: | 39652 |
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| Protein Theoretical pI: | 7 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Hydrogenase-2 small chain
MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECT
GCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGS
IPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVL
PGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDA
GRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGI
GFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGVSVMAVRELGR
QQKKDNADSRGE |
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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
- Sargent, F., Ballantine, S. P., Rugman, P. A., Palmer, T., Boxer, D. H. (1998). "Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit--identification of a soluble precursor of the small subunit in a hypB mutant." Eur J Biochem 255:746-754. Pubmed: 9738917
- Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314
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