ID   A0A6V8SIB4_9CLOT        Unreviewed;       551 AA.
AC   A0A6V8SIB4;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   10-FEB-2021, entry version 2.
DE   RecName: Full=Hydroxylamine reductase {ECO:0000256|HAMAP-Rule:MF_00069};
DE            EC=1.7.99.1 {ECO:0000256|HAMAP-Rule:MF_00069};
DE   AltName: Full=Hybrid-cluster protein {ECO:0000256|HAMAP-Rule:MF_00069};
DE            Short=HCP {ECO:0000256|HAMAP-Rule:MF_00069};
DE   AltName: Full=Prismane protein {ECO:0000256|HAMAP-Rule:MF_00069};
GN   Name=hcp {ECO:0000256|HAMAP-Rule:MF_00069};
GN   ORFNames=bsdtw1_03081 {ECO:0000313|EMBL:GFP76969.1};
OS   Clostridium sp. TW1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1604897 {ECO:0000313|EMBL:GFP76969.1};
RN   [1] {ECO:0000313|EMBL:GFP76969.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TW1 {ECO:0000313|EMBL:GFP76969.1};
RA   Ueki A., Tonouchi A.;
RT   "A new beta-1,3-glucan-decomposing anaerobic bacterium isolated from anoxic
RT   soil subjected to biological soil disinfestation.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and
CC       H(2)O. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00069};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00069};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00069};
CC   -!- COFACTOR:
CC       Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00069};
CC       Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000256|HAMAP-
CC       Rule:MF_00069};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00069}.
CC   -!- SIMILARITY: Belongs to the HCP family. {ECO:0000256|HAMAP-
CC       Rule:MF_00069}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GFP76969.1}.
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DR   EMBL; BLZR01000001; GFP76969.1; -; Genomic_DNA.
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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00069};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00069};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00069};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00069};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00069}.
FT   METAL           7
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           10
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           19
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           25
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           243
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           267
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           311
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           403
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           431
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           456
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           490
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   METAL           492
FT                   /note="Iron-oxo-sulfur (4Fe-2O-2S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
FT   MOD_RES         403
FT                   /note="Cysteine persulfide"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00069"
SQ   SEQUENCE   551 AA;  61523 MW;  631EA7EB62A3EEC4 CRC64;
     MENSMFCYQC EQTFGGKGCT KSGVCGKTPE IANLQDLLIY QLKGISCYAK PLIEQGKIID
     KEIVKFVENG LFTTLTNVNF DAEVHVRLLK ESQKIKEALR DEAPEGKYPD QATYDLSDTK
     EEMLRDSVKA GIMYDEDLNE DVRSLRSTIL YGLKGVSAYG HQARFIGYNS QQVDNIYFLG
     LEATTNDDLT VEELIRMTMR VGDMSVEVMK TLDDANTTRY SNPSPHKVNV NIVKGPFIIV
     SGHDLRDLEM LLEQTEGKGI NIYTHGEMLP SHGYKELKKY KHLVGNYGSA WQNQQKEFDG
     IPGCILMTTN CLMRPRETYK DRIFSTSVVG WDGIKHIDMK EDGTKDFSEI INKALELGGF
     KESEEEKEIL VGFGHHATLS HAETIVNAVK EGKIRHFFLI GGCDGARPGR NYYTDFAKMV
     PEDCVILTLA CGKYRFNKLD FGTVAGLPRL LDVGQCNDAY SAVRIATALA DAFDTSVNAL
     PLTIVLSWYE QKAVADLLAL LSLGIKGMYL GPSLPAFISP NVLQYLVDTF NIKPISTPED
     DLRSSLKQAM C
//