Identification
Name:Hydrogenase-1 small chain
Synonyms:
  • HYD1
  • Membrane-bound hydrogenase 1 small subunit
  • NiFe hydrogenase
Gene Name:hyaA
Enzyme Class:
Biological Properties
General Function:Involved in NADH dehydrogenase (ubiquinone) activity
Specific Function:This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth
Cellular Location:Cell inner membrane; Single-pass type I membrane protein; Periplasmic side
SMPDB Pathways:
KEGG Pathways:
  • Microbial metabolism in diverse environments ec01120
  • Trinitrotoluene degradation ec00633
KEGG Reactions:
2,4-Diamino-6-nitrotoluene2,4-Diamino-6-hydroxylaminotoluene
2,4-Diamino-6-nitrotoluene ↔ 2,4-Diamino-6-hydroxylaminotoluene
ReactionCard
Thumb+AcceptorReduced acceptor
Hydrogen (gas) + Acceptor ↔ Reduced acceptor
ReactionCard
SMPDB Reactions:
Thumb+Electron+2 Thumb+menaquinone-8Thumb+Thumb
Hydrogen ion + Electron + 2 Hydrogen ion + menaquinone-8 → Menaquinol 8 + Hydrogen ion
ReactionCard
Thumb+2 Thumb+Thumb
Complex Reactions:
2 Thumb+Thumb+ThumbThumb+2 Thumb
Thumb+2 Thumb+ThumbThumb+2 Thumb
2 Thumb+Thumb+Menaquinone 8Thumb+2 Thumb
Thumb+AAH(2)
Thumb+AAH(2)
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB01362Hydrogen (gas)MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
ferredoxin hydrogenase complex
macromolecular complex
protein complex
Function
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
metabolic process
oxidation reduction
Gene Properties
Blattner:b0972
Gene OrientationClockwise
Centisome Percentage:22.23
Left Sequence End1031362
Right Sequence End1032480
Gene Sequence:
>1119 bp
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Protein Properties
Pfam Domain Function:
Protein Residues:372
Protein Molecular Weight:40681
Protein Theoretical pI:7
Signaling Regions:
  • 1-45
Transmembrane Regions:
  • 326-348
Protein Sequence:
>Hydrogenase-1 small chain
MNNEETFYQAMRRQGVTRRSFLKYCSLAATSLGLGAGMAPKIAWALENKPRIPVVWIHGL
ECTCCTESFIRSAHPLAKDVILSLISLDYDDTLMAAAGTQAEEVFEDIITQYNGKYILAV
EGNPPLGEQGMFCISSGRPFIEKLKRAAAGASAIIAWGTCASWGCVQAARPNPTQATPID
KVITDKPIIKVPGCPPIPDVMSAIITYMVTFDRLPDVDRMGRPLMFYGQRIHDKCYRRAH
FDAGEFVQSWDDDAARKGYCLYKMGCKGPTTYNACSSTRWNDGVSFPIQSGHGCLGCAEN
GFWDRGSFYSRVVDIPQMGTHSTADTVGLTALGVVAAAVGVHAVASAVDQRRRHNQQPTE
TEHQPGNEDKQA
References
External Links:
ResourceLink
Uniprot ID:P69739
Uniprot Name:MBHS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062385
Ecogene ID:EG10468
Ecocyc:EG10468
ColiBase:b0972
Kegg Gene:b0972
EchoBASE ID:EB0463
CCDB:MBHS_ECOLI
BacMap:16128938
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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • 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
  • Menon, N. K., Robbins, J., Peck, H. D. Jr, Chatelus, C. Y., Choi, E. S., Przybyla, A. E. (1990). "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames." J Bacteriol 172:1969-1977. Pubmed: 2180913
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • 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