HCP_HALOH
ID HCP_HALOH Reviewed; 555 AA.
AC B8CZ59;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Hore_18290;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(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=[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; CP001098; ACL70578.1; -; Genomic_DNA.
DR RefSeq; WP_015923548.1; NC_011899.1.
DR AlphaFoldDB; B8CZ59; -.
DR SMR; B8CZ59; -.
DR STRING; 373903.Hore_18290; -.
DR EnsemblBacteria; ACL70578; ACL70578; Hore_18290.
DR KEGG; hor:Hore_18290; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_038344_2_0_9; -.
DR OMA; CAYAQGM; -.
DR OrthoDB; 337713at2; -.
DR Proteomes; UP000000719; 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..555
FT /note="Hydroxylamine reductase"
FT /id="PRO_1000118021"
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 248
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 272
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 316
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 408
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 436
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 461
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 496
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 498
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT MOD_RES 408
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
SQ SEQUENCE 555 AA; 61828 MW; FBFE15B6FAA83728 CRC64;
MSMFCFQCQE AARNKGCTVR GVCGKTGDVA NLQDLLVYLL KGISIYAEKA KELGVVDRET
GAFITRALFT TITNVNFDNK RFEEIIKEAF EVRDRIKNKF LKAYREKNGE EFDEKLPGMA
TWYSNDVSDF YAKGEEVGVL STGDEDVRAL RELLTYGLKG IAAYAEHAYI LEEEDQEIYS
FLQEGLVATT DNTLSADELT ALVMKCGEVA VKTMALLDQA NTSNYGHPEP TQVNLGVRNR
PGILVSGHDL KDLEELLEQT EGKGVDVYTH GEMLPANAYP AFKKYDHFVG NYGNAWWQQK
EEFEKFNGPI LMTTNCLVPP KDSYRDRVYT TNVVGFSGVK HIRDRKPGEQ KDFSPVIEHA
LKCDPPEELE NGMIPVGFAH NAVMSVADKV VEAVKQGKIK RFVVMAGCDG RHRSRDYYTN
VARNLPEDAV ILTAGCAKYR YNKLNLGDID GIPRILDAGQ CNDSYSLVVI AQKLAEVFGV
DDINELPISY DIAWYEQKAV AVLLALLYLG VKGIRLGPSL PAFLSPNVVK VLVDKFDIKP
IGEVEEDVKA IMAGE
