HCP1_CLOAB
ID HCP1_CLOAB Reviewed; 530 AA.
AC Q97FI7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Hydroxylamine reductase 1 {ECO:0000255|HAMAP-Rule:MF_00069};
DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069};
DE AltName: Full=Hybrid-cluster protein 1 {ECO:0000255|HAMAP-Rule:MF_00069};
DE Short=HCP 1 {ECO:0000255|HAMAP-Rule:MF_00069};
DE AltName: Full=Prismane protein 1 {ECO:0000255|HAMAP-Rule:MF_00069};
GN Name=hcp1 {ECO:0000255|HAMAP-Rule:MF_00069}; OrderedLocusNames=CA_C2750;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069};
CC Note=Binds 1 [4Fe-4S] 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; AE001437; AAK80696.1; -; Genomic_DNA.
DR PIR; E97238; E97238.
DR RefSeq; NP_349356.3; NC_003030.1.
DR RefSeq; WP_010966037.1; NC_003030.1.
DR AlphaFoldDB; Q97FI7; -.
DR SMR; Q97FI7; -.
DR STRING; 272562.CA_C2750; -.
DR PRIDE; Q97FI7; -.
DR EnsemblBacteria; AAK80696; AAK80696; CA_C2750.
DR GeneID; 44999238; -.
DR KEGG; cac:CA_C2750; -.
DR PATRIC; fig|272562.8.peg.2938; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_9; -.
DR OMA; CAYAQGM; -.
DR OrthoDB; 337713at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 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 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..530
FT /note="Hydroxylamine reductase 1"
FT /id="PRO_0000151670"
FT BINDING 5
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 227
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 251
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 295
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 384
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 412
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 437
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 472
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 474
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT MOD_RES 384
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
SQ SEQUENCE 530 AA; 58304 MW; F9E1644E53E98A2F CRC64;
MSMFCYQCQE AAGCKGCTVR GVCGKTEDLA KKQDLLIYTL KVVSLYNVEA RKLNLVNKEI
DNYIVDSLFA TITNANFDEN IFTERIEKGI KYKEELKKQI SAAGGNVNLN EKTEAVGVLS
TENEDIRSLR ELLTYGIKGM AAYLKHARNL SYEDSNIQGF MSKALAATLD DTLGADELVA
LALECGKYGV DAMALLDKAN TETYGNPEIT KVNIGTRNNP GILISGHDLK DIEELLKQTE
GTGVDVYTHS EMLPANYYPA FKKYSHFVGN YGNAWWKQNE EFESFNGPIL MTTNCIVPPK
ASYIDRMYTT GVTGYPGVKH IENGEPKDFS AIIEHAKKCA PPTEIEKGEI IGGFAHNQVI
ALADKVVEAV KSGAIKRFYV MAGCDGRAKT RNYYTDFAKA LPKDAVILTA GCAKYKYNKL
DLGDIGGIPR VLDAGQCNDS YSLVVIALKL KEVFGLNDIN ELPIAYNIAW YEQKAVIVLL
ALLHLGVKNI HLGPTLPAFL SPNVAKVLVD NFGIGGITNV EDDIKMFENL
