Identification |
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Name: | Formate hydrogenlyase subunit 5 |
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Synonyms: | - FHL subunit 5
- Hydrogenase-3 component E
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Gene Name: | hycE |
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Enzyme Class: | Not Available |
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Biological Properties |
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General Function: | Involved in oxidoreductase activity, acting on NADH or NADPH |
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Specific Function: | Specific function unknown |
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Cellular Location: | Not Available |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | Not Available |
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EcoCyc Reactions: | |
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Complex Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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binding | catalytic activity | cation binding | cofactor binding | ferredoxin hydrogenase activity | ion binding | metal ion binding | NAD or NADH binding | NADH dehydrogenase (quinone) activity | NADH dehydrogenase (ubiquinone) activity | NADH dehydrogenase activity | nickel ion binding | nucleotide binding | 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 | transition metal ion binding | Process |
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metabolic process | oxidation reduction |
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Gene Properties |
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Blattner: | b2721 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 61.27 |
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Left Sequence End | 2842784 |
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Right Sequence End | 2844493 |
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Gene Sequence: | >1710 bp
ATGTCTGAAGAAAAATTAGGTCAACATTATCTCGCCGCGCTGAATGAGGCATTTCCGGGC
GTCGTGCTGGACCACGCCTGGCAGACCAAAGATCAGCTGACTGTCACCGTAAAGGTGAAC
TACCTGCCGGAAGTGGTGGAGTTTCTTTACTACAAACAGGGTGGCTGGCTGTCGGTGCTG
TTTGGTAACGACGAACGCAAACTGAATGGTCATTACGCCGTTTACTACGTGCTGTCGATG
GAGAAGGGCACTAAGTGTTGGATTACGGTTCGCGTCGAAGTTGACGCCAACAAACCGGAA
TATCCGTCCGTGACGCCGCGCGTTCCGGCGGCGGTGTGGGGCGAGCGTGAAGTGCGCGAT
ATGTACGGTTTGATTCCGGTTGGTCTGCCGGATGAACGTCGTCTGGTGCTGCCGGATGAC
TGGCCGGATGAACTTTATCCGCTGCGTAAAGACAGCATGGATTATCGTCAGCGTCCGGCA
CCGACCACCGATGCTGAAACCTACGAGTTCATCAACGAACTGGGCGACAAGAAAAACAAC
GTCGTGCCGATTGGTCCGCTGCACGTCACTTCTGATGAACCGGGCCACTTCCGTCTGTTC
GTCGATGGCGAAAACATTATCGACGCCGACTACCGTCTGTTCTACGTCCATCGCGGCATG
GAAAAACTGGCGGAAACCCGTATGGGTTATAACGAAGTGACCTTCCTCTCTGACCGTGTG
TGCGGGATCTGCGGCTTTGCCCACAGCACCGCCTACACCACGTCGGTGGAAAACGCGATG
GGTATTCAGGTGCCAGAACGTGCGCAGATGATCCGCGCCATTCTGCTGGAGGTAGAACGC
TTGCACTCGCATCTGCTCAACCTTGGCCTGGCCTGTCACTTTACCGGCTTCGACTCCGGC
TTTATGCAGTTCTTCCGCGTGCGTGAAACCTCCATGAAAATGGCAGAGATCCTTACCGGT
GCGCGTAAAACCTACGGCCTGAACTTGATCGGCGGGATTCGTCGCGATCTGCTGAAAGAC
GACATGATCCAGACCCGCCAGCTGGCACAACAGATGCGTCGTGAAGTGCAGGAGCTGGTG
GATGTGCTGCTGAGCACTCCGAACATGGAACAGCGCACTGTCGGCATTGGTCGTCTGGAC
CCGGAAATCGCTCGCGACTTCAGTAACGTCGGCCCGATGGTCCGTGCCAGCGGTCACGCC
CGTGATACCCGCGCCGATCACCCGTTTGTCGGCTATGGCCTGCTGCCAATGGAAGTCCAC
AGCGAGCAGGGCTGCGACGTTATTTCCCGTCTGAAAGTGCGTATCAACGAAGTCTATACC
GCGCTGAACATGATCGACTACGGTCTGGATAACCTGCCGGGTGGCCCACTGATGGTGGAA
GGCTTTACCTACATTCCGCACCGCTTTGCGCTGGGCTTTGCCGAAGCGCCGCGCGGCGAT
GATATCCACTGGAGCATGACCGGCGACAACCAGAAGCTGTACCGCTGGCGCTGCCGTGCC
GCGACCTACGCGAACTGGCCGACCCTGCGCTACATGCTGCGCGGCAACACCGTTTCCGAT
GCGCCGCTGATTATCGGTAGCCTCGACCCTTGCTACTCCTGTACCGACCGCATGACCGTG
GTCGATGTGCGTAAGAAGAAGAGCAAAGTGGTGCCGTACAAAGAACTCGAGCGTTACAGC
ATTGAGCGTAAAAACTCGCCGCTGAAATAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 569 |
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Protein Molecular Weight: | 64980 |
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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: | >Formate hydrogenlyase subunit 5
MSEEKLGQHYLAALNEAFPGVVLDHAWQTKDQLTVTVKVNYLPEVVEFLYYKQGGWLSVL
FGNDERKLNGHYAVYYVLSMEKGTKCWITVRVEVDANKPEYPSVTPRVPAAVWGEREVRD
MYGLIPVGLPDERRLVLPDDWPDELYPLRKDSMDYRQRPAPTTDAETYEFINELGDKKNN
VVPIGPLHVTSDEPGHFRLFVDGENIIDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRV
CGICGFAHSTAYTTSVENAMGIQVPERAQMIRAILLEVERLHSHLLNLGLACHFTGFDSG
FMQFFRVRETSMKMAEILTGARKTYGLNLIGGIRRDLLKDDMIQTRQLAQQMRREVQELV
DVLLSTPNMEQRTVGIGRLDPEIARDFSNVGPMVRASGHARDTRADHPFVGYGLLPMEVH
SEQGCDVISRLKVRINEVYTALNMIDYGLDNLPGGPLMVEGFTYIPHRFALGFAEAPRGD
DIHWSMTGDNQKLYRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRMTV
VDVRKKKSKVVPYKELERYSIERKNSPLK |
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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
- Bohm, R., Sauter, M., Bock, A. (1990). "Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components." Mol Microbiol 4:231-243. Pubmed: 2187144
- 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
- Rossmann, R., Sauter, M., Lottspeich, F., Bock, A. (1994). "Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537." Eur J Biochem 220:377-384. Pubmed: 8125094
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