ID   HIS3_LEPIN              Reviewed;         187 AA.
AC   Q8F8K4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI; OrderedLocusNames=LA_0551;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000305}.
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DR   EMBL; AE010300; AAN47750.1; -; Genomic_DNA.
DR   RefSeq; NP_710732.1; NC_004342.2.
DR   RefSeq; WP_000098501.1; NC_004342.2.
DR   AlphaFoldDB; Q8F8K4; -.
DR   SMR; Q8F8K4; -.
DR   STRING; 189518.LA_0551; -.
DR   EnsemblBacteria; AAN47750; AAN47750; LA_0551.
DR   KEGG; lil:LA_0551; -.
DR   PATRIC; fig|189518.3.peg.556; -.
DR   HOGENOM; CLU_1446017_0_0_12; -.
DR   InParanoid; Q8F8K4; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.810; -; 1.
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; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..187
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /id="PRO_0000136480"
SQ   SEQUENCE   187 AA;  21653 MW;  1CDDA75563E31373 CRC64;
     MSSREITILK IQEPTRSIAS LTRIMEEELS QYRKTLPKGF REEVDCDEDT VLFLHVDFLP
     LDFQKTTELL LTGKKNLVPV VAIDLQGQIL MQAFGNEESQ TLSLKTGYAH YFSRSRNQLW
     KKGDTSGHTQ KILQILSPTD RSFLVYQVEQ EVAACHEGYY SCFFRERMEG VTWKLLPVPR
     NFLPEKS