ID A0A0F4EQN9_9MYCO Unreviewed; 115 AA. AC A0A0F4EQN9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 22-FEB-2023, entry version 28. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021, GN ECO:0000313|EMBL:KJX75218.1}; GN ORFNames=MLPM_1264 {ECO:0000313|EMBL:KJX75218.1}; OS Mycobacterium lepromatosis. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=480418 {ECO:0000313|EMBL:KJX75218.1, ECO:0000313|Proteomes:UP000053699}; RN [1] {ECO:0000313|EMBL:KJX75218.1, ECO:0000313|Proteomes:UP000053699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mx1-22A {ECO:0000313|EMBL:KJX75218.1, RC ECO:0000313|Proteomes:UP000053699}; RX PubMed=25831531; DOI=10.1073/pnas.1421504112; RA Singh P., Benjak A., Schuenemann V.J., Herbig A., Avanzi C., Busso P., RA Nieselt K., Krause J., Vera-Cabrera L., Cole S.T.; RT "Insight into the evolution and origin of leprosy bacilli from the genome RT sequence of Mycobacterium lepromatosis."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4459-4464(2015). CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta- CC D-ribosyl)-5-[(5-phospho-beta-D- CC ribosylamino)methylideneamino]imidazole-4-carboxamide; CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, CC ChEBI:CHEBI:59457; EC=3.5.4.19; CC Evidence={ECO:0000256|ARBA:ARBA00000024, ECO:0000256|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01021}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01021}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01021}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC {ECO:0000256|ARBA:ARBA00005169, ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP- CC Rule:MF_01021}. 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:KJX75218.1}. 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; JRPY01000050; KJX75218.1; -; Genomic_DNA. DR RefSeq; WP_045843022.1; NZ_JRPY01000050.1. DR AlphaFoldDB; A0A0F4EQN9; -. DR STRING; 480418.GCA_000975265_01335; -. DR EnsemblBacteria; KJX75218; KJX75218; MLPM_1264. DR PATRIC; fig|480418.6.peg.2541; -. DR OrthoDB; 9795769at2; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000053699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1. DR HAMAP; MF_01021; HisI; 1. DR InterPro; IPR026660; PRA-CH. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf. DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR42945:SF11; PHOSPHORIBOSYL-AMP CYCLOHYDROLASE; 1. DR Pfam; PF01502; PRA-CH; 1. DR SUPFAM; SSF141734; HisI-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_01021}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01021}; KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP- KW Rule:MF_01021}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01021}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01021}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01021}. FT DOMAIN 33..105 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT /evidence="ECO:0000259|Pfam:PF01502" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" FT BINDING 84 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01021" SQ SEQUENCE 115 AA; 12522 MW; 806D80D0C1B2FCC9 CRC64; MTLDPDIAAR LKRNAEGLFT AVVQERSSGD VLMVAWMDDQ ALARTLETRE ANYYSRSRAE QWIKGATSGN TQHVHSVRLD CDGDTVLLTV DQVGGACHTG AHSCFDAAML LAPQD //