HCP_MANSM
ID HCP_MANSM Reviewed; 553 AA.
AC Q65VW2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MS0291;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU36898.1; -; Genomic_DNA.
DR RefSeq; WP_011199473.1; NC_006300.1.
DR AlphaFoldDB; Q65VW2; -.
DR SMR; Q65VW2; -.
DR STRING; 221988.MS0291; -.
DR EnsemblBacteria; AAU36898; AAU36898; MS0291.
DR KEGG; msu:MS0291; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_6; -.
DR OMA; CAYAQGM; -.
DR OrthoDB; 337713at2; -.
DR Proteomes; UP000000607; 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 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..553
FT /note="Hydroxylamine reductase"
FT /id="PRO_1000009156"
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 459
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 493
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 495
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 553 AA; 60851 MW; C6823D3A763A5850 CRC64;
MYCVQCEQTM VTPKGNGCSF SQGMCGKTAE TSDLQDLLIA TLHSLSAWAL KAREHNIIIH
EADAFAPRAF FATLTNVNFD SARIAGYAQQ ALIYRNQLIK AVNEVEPNPN IDHPLANIEL
NGISVEQLAL QAKQFALDTD RQQIGEEAHG VRLLCLYGLK GAAAYMEHAY VLDKFDNDIY
AEYHGFMSWL GTQPGDLNEL LEKALAIGSM NFKVMAMLDA GETEHFGNPV PAMVNVRPVK
GKCILISGHD LKDLKELLEQ TEGKGINVYT HGEMLPAHGY PELKKYKHLV GNFGSGWQNQ
QKEFARFPGA IVMTSNCLID PNVGDYADRI FTRNIVGWPG VTHLEDHDFS PVIEKALQCD
GFPYTELEHL ITVGFGRKTL IDASDAVIDL VKAGKLSHVF VIGGCDGDKE ERHYYTDLAY
ALPKDTAVLT LGCGKYRFNK LDFGTIDGGL PRLLDAGQCN DTYSAIMLAV TLSQKLGIGL
NELPLSIVLS WFEQKAIIVL LTLLALGVKN VYSGPSKPAF LNDNVMALLH EKFGLSGLTT
PEQDFGHIIN KNL
