HCP_RHOCA
ID HCP_RHOCA Reviewed; 546 AA.
AC Q6WRT6;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Hydroxylamine reductase {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000303|PubMed:15322098};
DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:15322098};
DE AltName: Full=Hybrid-cluster protein {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000303|PubMed:15322098};
DE Short=HCP {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000303|PubMed:15322098};
DE AltName: Full=Prismane protein {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000303|PubMed:15322098};
GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000303|PubMed:15322098};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC STRAIN=B10S, and E1F1;
RX PubMed=15322098; DOI=10.1074/jbc.m404417200;
RA Cabello P., Pino C., Olmo-Mira M.F., Castillo F., Roldan M.D.,
RA Moreno-Vivian C.;
RT "Hydroxylamine assimilation by Rhodobacter capsulatus E1F1. requirement of
RT the hcp gene (hybrid cluster protein) located in the nitrate assimilation
RT nas gene region for hydroxylamine reduction.";
RL J. Biol. Chem. 279:45485-45494(2004).
CC -!- FUNCTION: Could be involved in assimilation and/or detoxification of
CC hydroxylamine, which is a toxic compound that may be formed during
CC nitrate/nitrite assimilation. Catalyzes the reduction of hydroxylamine
CC to form NH(3) and H(2)O. It has a low reductase activity with FAD, FMN,
CC benzyl viologen and bromphenol blue as electrons donors, but it is not
CC able to use NAD or NADP. {ECO:0000269|PubMed:15322098}.
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, ECO:0000269|PubMed:15322098};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:15322098};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:15322098};
CC -!- COFACTOR:
CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:15322098};
CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000255|HAMAP-
CC Rule:MF_00069, ECO:0000269|PubMed:15322098};
CC -!- ACTIVITY REGULATION: Inhibited by cyanide and by sulfide and iron
CC reagents such as dithioerythritol, 2,2'-dipyridyl and o-phenanthroline.
CC {ECO:0000269|PubMed:15322098}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for methyl viologen (at pH 9.3 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:15322098};
CC KM=1 mM for hydroxylamine (at pH 9.3 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:15322098};
CC pH dependence:
CC Optimum pH i 9.3. {ECO:0000269|PubMed:15322098};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:15322098};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069,
CC ECO:0000269|PubMed:15322098}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow with
CC hydroxylamine as the sole nitrogen source.
CC {ECO:0000269|PubMed:15322098}.
CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP-
CC Rule:MF_00069, ECO:0000305}.
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DR EMBL; AY273169; AAQ18177.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WRT6; -.
DR SMR; Q6WRT6; -.
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 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..546
FT /note="Hydroxylamine reductase"
FT /id="PRO_0000430413"
FT BINDING 3
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 6
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 245
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 269
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 313
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 401
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 429
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 454
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 488
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT BINDING 490
FT /ligand="hybrid [4Fe-2O-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:60519"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
FT MOD_RES 401
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00069"
SQ SEQUENCE 546 AA; 58206 MW; 44FEAD018E856228 CRC64;
MYCIQCEQTL HTATGTGCRF ARGDCGKTAA ISDQQDALVA ALLAVSSHAD AARKVGLIDA
EVDAFVPQAL FATLTNVNFD PERLAGYIRK AQELRNRLQL ALAGKPLALP ALADADWPFA
AAQQAEAGKI VALNRDAARI GEDVLGLRLL CLYGLKGIAA YMEHARVLGQ TDTQVAAGFH
AHMAYLASEP TDAKGLFAEA LAIGTLNFRV MEMLDAGATG TFGDPQPTPV NRRPVAGKAI
LVSGHDLHDL LRILEQTAGR GINVYTHGEM LPAHGYPAFH AHPHLIGNYG SAWQNQQAEF
AAFPGAIVMT SNCLIDPRTG AYQDRIFTRS IVGWPGVRHI EGEDFAEVIA CAEALPGFAA
TEAPVTQLTG FGRNALMTAA PAVIERVKVG KIRHFYLIGG CDGARAERAY YADLARMLPQ
DTVVLTLGCG KFRLDGIDFG AVDGLPRLLD VGQCNDAYAA IRLALALAEA FDCGVNDLPL
TLVLSWFEQK AIVILLTLLA LGVKDIRVGP TAPGFLTPNL IATLNAQFGL RLISTPEETM
AETLSA
