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HCP_SALG2
ID   HCP_SALG2               Reviewed;         550 AA.
AC   B5R885;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=SG0880;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR36773.1; -; Genomic_DNA.
DR   RefSeq; WP_000458795.1; NC_011274.1.
DR   AlphaFoldDB; B5R885; -.
DR   SMR; B5R885; -.
DR   EnsemblBacteria; CAR36773; CAR36773; SG0880.
DR   KEGG; seg:SG0880; -.
DR   HOGENOM; CLU_038344_2_0_6; -.
DR   OMA; CAYAQGM; -.
DR   Proteomes; UP000008321; 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_1000092347"
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;  60104 MW;  B678DA7883E2DA73 CRC64;
     MFCVQCEQTI RTPAGNGCSY AQGMCGKTAE TSDLQDLLIA ALQGLSAWAV KAREYGIINH
     DVDNFAPRSF FSTLTNVNFD SPRIVGYARE AIALREALKA QCLSVDANAH CDNPMADLQL
     VSDDLGELQR QAAEFTPNKD KAAIGENILG LRLLCLYGLK GAAAYMEHAH VLGQYDNDIY
     AQYHKIMAWL GTWPADMNAL LECAMEIGQM NFKVMSILDA GETTKYGHPT PTQVNVKATE
     GKCILISGHD LKDLYNLLEQ TEGTGVNVYT HGEMLPAHGY PELRKFKHLV GNYGSGWQNQ
     QVEFARFPGP IVMTSNCIID PTVGSYDDRI WTRSIVGWPG VSHLEGDDFG PVIAQAQQMA
     GFPYSEIPHL ITVGFGRQTL LGAADTLIDL VSREKLRHIF LVGGCDGARG ERNYFTDFAT
     SVPDDCLILT LACGKYRFNK LEFGDIEGLP RLVDAGQCND AYSAIILAVT LAEKLGCGVN
     DLPLSLVLSW FEQKAIVILL TLLSLGVKNI VTGPTAPGFF TPDLLAVLNE KFGLRSVTTV
     EEDMKQLLSA
 
 
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