ID   A0A0F4EQN9_9MYCO        Unreviewed;       115 AA.
AC   A0A0F4EQN9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   02-DEC-2020, entry version 22.
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}.
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DR   EMBL; JRPY01000050; KJX75218.1; -; Genomic_DNA.
DR   RefSeq; WP_045843022.1; NZ_LAWX01000023.1.
DR   EnsemblBacteria; KJX75218; KJX75218; MLPM_1264.
DR   PATRIC; fig|480418.6.peg.2541; -.
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; 3.10.20.400; -; 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   Pfam; PF01502; PRA-CH; 1.
DR   SUPFAM; SSF141734; SSF141734; 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   ECO:0000313|EMBL:KJX75218.1}; 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="PRA-CH"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
FT   METAL           80
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   METAL           81
FT                   /note="Zinc; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   METAL           82
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   METAL           84
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   METAL           97
FT                   /note="Zinc; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01021"
FT   METAL           104
FT                   /note="Zinc; shared with dimeric partner"
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
//