ID B7JGC0_BACC0 Unreviewed; 436 AA. AC B7JGC0; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 84. 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 OrderedLocusNames=BCAH820_3458 {ECO:0000313|EMBL:ACK91399.1}; OS Bacillus cereus (strain AH820). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK91399.1, ECO:0000313|Proteomes:UP000001363}; RN [1] {ECO:0000313|EMBL:ACK91399.1, ECO:0000313|Proteomes:UP000001363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820 {ECO:0000313|EMBL:ACK91399.1, RC ECO:0000313|Proteomes:UP000001363}; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH820."; RL Submitted (OCT-2008) 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 --------------------------------------------------------------------------- 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; CP001283; ACK91399.1; -; Genomic_DNA. DR AlphaFoldDB; B7JGC0; -. DR KEGG; bcu:BCAH820_3458; -. DR HOGENOM; CLU_038344_0_0_9; -. DR Proteomes; UP000001363; 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 Gene3D; 1.20.1270.20; -; 1. 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 NCBIfam; TIGR01703; hybrid_clust; 1. DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1. DR PANTHER; PTHR30109:SF0; HYDROXYLAMINE REDUCTASE; 1. DR Pfam; PF03063; Prismane; 2. DR SUPFAM; SSF56821; Prismane protein-like; 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 BINDING 11 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 14 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 22 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 28 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 136 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 160 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 204 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 290 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /note="via persulfide group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 318 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 345 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 379 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT BINDING 381 FT /ligand="hybrid [4Fe-2O-2S] cluster" FT /ligand_id="ChEBI:CHEBI:60519" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" FT MOD_RES 290 FT /note="Cysteine persulfide" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00069" SQ SEQUENCE 436 AA; 48154 MW; A7AE3F1A77454F70 CRC64; MIGRGWDDMF CYQCEQTPTG GCKVMGVCGK NETIASLQDT IVFGLKGIAA YRTHAAQLGY TDAFVDATTQ EALYMTLTNS NFNEQEHVDM AMKVGKSALR VMELLDEAHT NHFGVPEPVQ ITQNRVEGKA IVVTGHNLFA LEELLKQTEG KEINIYTHSE MLPAHGYPQL KKYKHLKGNI GKAWYDQRRL FEKFTGAILA TTNCVMPIKG SYSDRFFSYD IAGLEGVQKI ENDNFAPLIQ KALELPEVHM ESDEQLVTGF HHNTVLSLAP EIIEAVKEGK IKRFFVIAGC DAPGKGGEYY RELATSLPPE TVILTTSCGK FRFNDVDYGV VPGTEIPRYI DLGQCNNSIS TVKIAAALAD AFQCEVNELP VSIVLSWFEQ KAVAILLGLF SLGIQDIRIG PKAPEFISAG VLDVLQETFG LKLITTAAED MEMMLS //