HCP_ECO27
ID HCP_ECO27 Reviewed; 550 AA.
AC B7UMW5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Hydroxylamine reductase {ECO:0000255|HAMAP-Rule:MF_00069};
DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069};
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:0000255|HAMAP-Rule:MF_00069};
GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069}; OrderedLocusNames=E2348C_0870;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and
CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00069}.
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};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00069};
CC -!- COFACTOR:
CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069};
CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000255|HAMAP-
CC Rule:MF_00069};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}.
CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP-
CC Rule:MF_00069}.
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DR EMBL; FM180568; CAS08418.1; -; Genomic_DNA.
DR RefSeq; WP_000458817.1; NC_011601.1.
DR AlphaFoldDB; B7UMW5; -.
DR SMR; B7UMW5; -.
DR EnsemblBacteria; CAS08418; CAS08418; E2348C_0870.
DR GeneID; 66670853; -.
DR KEGG; ecg:E2348C_0870; -.
DR HOGENOM; CLU_038344_2_0_6; -.
DR OMA; CAYAQGM; -.
DR Proteomes; UP000008205; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..550
FT /note="Hydroxylamine reductase"
FT /id="PRO_1000118018"
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"
SQ SEQUENCE 550 AA; 60048 MW; 4B539878F663FC82 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 VRHLDGEDFS AVIAQAQQMA
GFPYSEIPHL ITVGFGRQTL LGAADTLIDL VSREKLRHIF LLGGCDGARG ERHYFTDFAT
SVPDDCLILT LACGKYRFNK LEFGDIEGLP RLVDAGQCND AYSAIILAVT LAEKLGCGVN
DLPLSLVLSW FEQKAIVILL TLLSLGVKNI VTGPTAPGFL TPDLLAVLNE KFGLRSITTV
EEDMKQLLSA
