ID   A0A0F4EQN9_9MYCO        Unreviewed;       115 AA.
AC   A0A0F4EQN9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-JUN-2016, entry version 9.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00006950};
DE            Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00103216};
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
RT   genome 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       ECO:0000256|SAAS:SAAS00103149}.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1-
CC       (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-
CC       ribosylamino)methylideneamino)imidazole-4-carboxamide.
CC       {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00103132}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01021};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01021};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01021};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01021};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00103190}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00103178}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00006977}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01021, ECO:0000256|SAAS:SAAS00578260}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   Proteomes; UP000053699; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01021; HisI; 1.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00469223};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053699};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00419140};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00469264};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00469262, ECO:0000313|EMBL:KJX75218.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00419138};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00419151};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00419177}.
FT   DOMAIN       33    105       PRA-CH. {ECO:0000259|Pfam:PF01502}.
FT   METAL        80     80       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        81     81       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL        82     82       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        84     84       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        97     97       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL       104    104       Zinc; shared with dimeric partner.
FT                                {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
//