ID A0A6V8SIB4_9CLOT Unreviewed; 551 AA. AC A0A6V8SIB4; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 02-JUN-2021, entry version 4. 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; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1604897 {ECO:0000313|EMBL:GFP76969.1, ECO:0000313|Proteomes:UP000580568}; RN [1] {ECO:0000313|EMBL:GFP76969.1, ECO:0000313|Proteomes:UP000580568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW1 {ECO:0000313|EMBL:GFP76969.1, RC ECO:0000313|Proteomes:UP000580568}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BLZR01000001; GFP76969.1; -; Genomic_DNA. DR Proteomes; UP000580568; Unassembled WGS sequence. 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 {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 //