Hydroxylamine reductase (P75825)

Identification
Name:Hydroxylamine reductase
Synonyms:
  • Hybrid-cluster protein
  • HCP
Gene Name:hcp
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on other nitrogenous compounds as donors
Specific Function:Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Acceptor ↔ 1.0Thumb+1.0Reduced acceptor
1.0Ammonia + 1.0Water + 1.0Acceptor ↔ 1.0Hydroxylamine + 1.0Reduced acceptor
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0cytochrome c nitrite reductase ↔ 1.0Thumb+1.0Thumb+1.0cytochrome c nitrite reductase
1.0Hydroxylamine + 1.0cytochrome c nitrite reductase ↔ 1.0Ammonia + 1.0Water + 1.0cytochrome c nitrite reductase
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0an oxidized electron acceptor ← 1.0a reduced electron acceptor+1.0hydroxylamine
1.0Ammonia + 1.0Water + 1.0an oxidized electron acceptor ← 1.0a reduced electron acceptor + 1.0hydroxylamine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21444HydroxylamineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
oxidoreductase activity, acting on other nitrogenous compounds as donors
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0873
Gene OrientationCounterclockwise
Centisome Percentage:19.64
Left Sequence End911385
Right Sequence End913037
Gene Sequence:
>1653 bp
ATGAAATTATTGCAGCGGGGCGTGGCGTTAGCGCTGTTAACCACATTTACACTGGCGAGT
GAAACTGCTCTGGCGTATGAGCAGGATAAAACCTACAAAATTACAGTTCTGCATACCAAT
GATCATCATGGGCATTTTTGGCGCAATGAATATGGCGAATATGGTCTGGCGGCGCAAAAA
ACGCTGGTGGATGGTATCCGCAAAGAGGTTGCGGCTGAAGGCGGTAGCGTGCTGCTACTT
TCCGGTGGCGACATTAACACTGGCGTGCCCGAGTCTGACTTACAGGATGCCGAACCTGAT
TTTCGCGGTATGAATCTGGTGGGCTATGACGCGATGGCGATCGGTAATCATGAATTTGAT
AATCCGCTCACCGTATTACGCCAGCAGGAAAAGTGGGCCAAGTTCCCGTTGCTTTCCGCG
AATATCTACCAGAAAAGTACTGGCGAGCGCCTGTTTAAACCGTGGGCGCTGTTTAAGCGT
CAGGATCTGAAAATTGCCGTTATTGGGCTGACAACCGATGACACAGCAAAAATTGGTAAC
CCGGAATACTTCACTGATATCGAATTTCGTAAGCCCGCCGATGAAGCGAAGCTGGTGATT
CAGGAGCTGCAACAGACAGAAAAGCCAGACATTATTATCGCGGCGACCCATATGGGGCAT
TACGATAATGGTGAGCACGGCTCTAACGCACCGGGCGATGTGGAGATGGCACGCGCGCTG
CCTGCCGGATCGCTGGCGATGATCGTCGGTGGTCACTCGCAAGATCCGGTCTGCATGGCG
GCAGAAAACAAAAAACAGGTCGATTACGTGCCGGGTACGCCATGCAAACCAGATCAACAA
AACGGCATCTGGATTGTGCAGGCGCATGAGTGGGGCAAATACGTGGGACGGGCTGATTTT
GAGTTTCGTAATGGCGAAATGAAAATGGTTAACTACCAGCTGATTCCGGTGAACCTGAAG
AAGAAAGTGACCTGGGAAGACGGGAAAAGCGAGCGCGTGCTTTACACTCCTGAAATCGCT
GAAAACCAGCAAATGATCTCGCTGTTATCACCGTTCCAGAACAAAGGCAAAGCGCAGCTG
GAAGTGAAAATAGGCGAAACCAATGGTCGTCTGGAAGGCGATCGTGACAAAGTGCGTTTT
GTACAGACCAATATGGGGCGGTTGATTCTGGCAGCCCAAATGGATCGCACTGGTGCCGAC
TTTGCGGTGATGAGCGGAGGCGGAATTCGTGATTCTATCGAAGCAGGCGATATCAGCTAT
AAAAACGTGCTGAAAGTGCAGCCATTCGGCAATGTGGTGGTGTATGCCGACATGACCGGT
AAAGAGGTGATTGATTACCTGACCGCCGTCGCGCAGATGAAGCCAGATTCAGGTGCCTAC
CCGCAATTTGCCAACGTTAGCTTTGTGGCGAAAGACGGCAAACTGAACGACCTTAAAATC
AAAGGCGAACCGGTCGATCCGGCGAAAACTTACCGTATGGCGACATTAAACTTCAATGCC
ACCGGCGGTGATGGATATCCGCGCCTTGATAACAAACCGGGCTATGTGAATACCGGCTTT
ATTGATGCCGAAGTGCTGAAAGCGTATATCCAGAAAAGCTCGCCGCTGGATGTGAGTGTT
TATGAACCGAAAGGTGAGGTGAGCTGGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:550
Protein Molecular Weight:60063
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Hydroxylamine reductase
MFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIAALQGLSAWAVKAREYGIINH
DVDSFAPRAFFSTLTNVNFDSPRIVGYAREAIALREALKAQCLAVDANARVDNPMADLQL
VSDDLGELQRQAAEFTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNDIY
AQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA
GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQ
QVEFARFPGPIVMTSNCIIDPTVGAYDDRIWTRSIVGWPGVRHLDGDDFSAVITQAQQMA
GFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFAT
SVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVN
DLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTV
EEDMKQLLSA
References
External Links:
ResourceLink
Uniprot ID:P75825
Uniprot Name:HCP_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674619
Ecogene ID:EG13692
Ecocyc:EG13692
ColiBase:b0873
Kegg Gene:b0873
EchoBASE ID:EB3456
CCDB:HCP_ECOLI
BacMap:90111180
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
  • 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
  • van den Berg, W. A., Hagen, W. R., van Dongen, W. M. (2000). "The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]." Eur J Biochem 267:666-676. Pubmed: 10651802
  • Wolfe, M. T., Heo, J., Garavelli, J. S., Ludden, P. W. (2002). "Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli." J Bacteriol 184:5898-5902. Pubmed: 12374823