HCP_ECOLI
ID HCP_ECOLI Reviewed; 550 AA.
AC P75825; Q9R7R0; Q9R7R1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Hydroxylamine reductase {ECO:0000303|PubMed:12374823};
DE EC=1.7.99.1 {ECO:0000269|PubMed:12374823};
DE AltName: Full=Hybrid-cluster protein {ECO:0000255|HAMAP-Rule:MF_00069};
DE Short=HCP {ECO:0000255|HAMAP-Rule:MF_00069};
DE AltName: Full=Prismane protein {ECO:0000303|PubMed:10651802};
GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069}; Synonyms=ybjW;
GN OrderedLocusNames=b0873, JW0857;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 134.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP COFACTOR.
RX PubMed=10381368; DOI=10.1006/bbrc.1999.0748;
RA Pereira A.S., Tavares P., Krebs C., Huynh B.H., Rusnak F., Moura I.,
RA Moura J.J.;
RT "Biochemical and spectroscopic characterization of overexpressed
RT fuscoredoxin from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 260:209-215(1999).
RN [5]
RP FUNCTION, AND COFACTOR.
RX PubMed=10651802; DOI=10.1046/j.1432-1327.2000.01032.x;
RA van den Berg W.A.M., Hagen W.R., van Dongen W.M.A.M.;
RT "The hybrid-cluster protein ('prismane protein') from Escherichia coli.
RT Characterization of the hybrid-cluster protein, redox properties of the
RT [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH
RT oxidoreductase containing FAD and 2Fe-2S.";
RL Eur. J. Biochem. 267:666-676(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=12374823; DOI=10.1128/jb.184.21.5898-5902.2002;
RA Wolfe M.T., Heo J., Garavelli J.S., Ludden P.W.;
RT "Hydroxylamine reductase activity of the hybrid cluster protein from
RT Escherichia coli.";
RL J. Bacteriol. 184:5898-5902(2002).
RN [7]
RP INDUCTION.
RX PubMed=15667305; DOI=10.1042/bst0330195;
RA Filenko N.A., Browning D.F., Cole J.A.;
RT "Transcriptional regulation of a hybrid cluster (prismane) protein.";
RL Biochem. Soc. Trans. 33:195-197(2005).
CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and
CC H(2)O. Is also able to reduce hydroxylamine analogs such as
CC methylhydroxylamine and hydroxyquinone. Might have a role as a
CC scavenger of potentially toxic by-products of nitrate metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:10651802,
CC ECO:0000269|PubMed:12374823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine;
CC Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:28938; EC=1.7.99.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00069, ECO:0000269|PubMed:12374823};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:10381368, ECO:0000269|PubMed:10651802};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:10381368, ECO:0000269|PubMed:10651802};
CC -!- COFACTOR:
CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:10381368, ECO:0000269|PubMed:10651802};
CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000255|HAMAP-
CC Rule:MF_00069, ECO:0000269|PubMed:10381368,
CC ECO:0000269|PubMed:10651802};
CC -!- ACTIVITY REGULATION: Inhibited by oxygen. Activated by cyanide except
CC in the prolonged presence of excess cyanide, where the enzyme is
CC inactivated. {ECO:0000269|PubMed:12374823}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for hydroxylamine (at pH 9) {ECO:0000269|PubMed:12374823};
CC Vmax=92 umol/min/mg enzyme (at pH 7.5) {ECO:0000269|PubMed:12374823};
CC Vmax=458 umol/min/mg enzyme (at pH 9) {ECO:0000269|PubMed:12374823};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:12374823};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}.
CC -!- INDUCTION: By Fnr, NarL and NarP under anaerobic conditions in the
CC presence of either nitrate or nitrite. {ECO:0000269|PubMed:15667305}.
CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP-
CC Rule:MF_00069}.
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DR EMBL; U00096; AAC73960.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35587.2; -; Genomic_DNA.
DR PIR; A64826; A64826.
DR RefSeq; NP_415394.4; NC_000913.3.
DR RefSeq; WP_000458809.1; NZ_SSZK01000002.1.
DR PDB; 7DE4; X-ray; 3.61 A; A=1-550.
DR PDBsum; 7DE4; -.
DR AlphaFoldDB; P75825; -.
DR SMR; P75825; -.
DR BioGRID; 4262100; 10.
DR BioGRID; 850939; 4.
DR DIP; DIP-9870N; -.
DR IntAct; P75825; 5.
DR STRING; 511145.b0873; -.
DR jPOST; P75825; -.
DR PaxDb; P75825; -.
DR PRIDE; P75825; -.
DR EnsemblBacteria; AAC73960; AAC73960; b0873.
DR EnsemblBacteria; BAA35587; BAA35587; BAA35587.
DR GeneID; 946592; -.
DR KEGG; ecj:JW0857; -.
DR KEGG; eco:b0873; -.
DR PATRIC; fig|1411691.4.peg.1404; -.
DR EchoBASE; EB3456; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_6; -.
DR InParanoid; P75825; -.
DR OMA; CAYAQGM; -.
DR PhylomeDB; P75825; -.
DR BioCyc; EcoCyc:G6457-MON; -.
DR BioCyc; MetaCyc:G6457-MON; -.
DR PRO; PR:P75825; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050418; F:hydroxylamine reductase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0004601; F:peroxidase activity; IDA:EcoliWiki.
DR GO; GO:0046210; P:nitric oxide catabolic process; IMP:EcoCyc.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:EcoCyc.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:EcoCyc.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; IDA:EcoCyc.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:EcoliWiki.
DR CDD; cd01914; HCP; 1.
DR Gene3D; 1.20.1270.20; -; 2.
DR Gene3D; 3.40.50.2030; -; 2.
DR HAMAP; MF_00069; Hydroxylam_reduct; 1.
DR InterPro; IPR004137; HCP/CODH.
DR InterPro; IPR010048; Hydroxylam_reduct.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR InterPro; IPR016100; Prismane_a-bundle.
DR PANTHER; PTHR30109; PTHR30109; 1.
DR PANTHER; PTHR30109:SF0; PTHR30109:SF0; 1.
DR Pfam; PF03063; Prismane; 1.
DR PIRSF; PIRSF000076; HCP; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR01703; hybrid_clust; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..550
FT /note="Hydroxylamine reductase"
FT /id="PRO_0000151674"
FT BINDING 3
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 6
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 18
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 25
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 249
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 273
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 317
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 405
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /note="via persulfide group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 433
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 458
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 492
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 494
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT MOD_RES 405
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT CONFLICT 134
FT /note="E -> V (in Ref. 1; AAC73960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 60064 MW; CA4958B3143B1F48 CRC64;
MFCVQCEQTI RTPAGNGCSY AQGMCGKTAE TSDLQDLLIA ALQGLSAWAV KAREYGIINH
DVDSFAPRAF FSTLTNVNFD SPRIVGYARE AIALREALKA QCLAVDANAR VDNPMADLQL
VSDDLGELQR QAAEFTPNKD KAAIGENILG LRLLCLYGLK GAAAYMEHAH VLGQYDNDIY
AQYHKIMAWL GTWPADMNAL LECSMEIGQM NFKVMSILDA GETGKYGHPT PTQVNVKATA
GKCILISGHD LKDLYNLLEQ TEGTGVNVYT HGEMLPAHGY PELRKFKHLV GNYGSGWQNQ
QVEFARFPGP IVMTSNCIID PTVGAYDDRI WTRSIVGWPG VRHLDGDDFS AVITQAQQMA
GFPYSEIPHL ITVGFGRQTL LGAADTLIDL VSREKLRHIF LLGGCDGARG ERHYFTDFAT
SVPDDCLILT LACGKYRFNK LEFGDIEGLP RLVDAGQCND AYSAIILAVT LAEKLGCGVN
DLPLSLVLSW FEQKAIVILL TLLSLGVKNI VTGPTAPGFL TPDLLAVLNE KFGLRSITTV
EEDMKQLLSA
