ID   HIS4_MYCTO              Reviewed;         244 AA.
AC   P9WMM4; L0T7E1; O06588; P60578;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Phosphoribosyl isomerase A;
DE   AltName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE            EC=5.3.1.16;
DE   AltName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN   Name=priA; Synonyms=hisA; OrderedLocusNames=MT1639;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in both the histidine and tryptophan biosynthetic
CC       pathways. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC         phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC         ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC         carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC         EC=5.3.1.24;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45907.1; -; Genomic_DNA.
DR   PIR; E70544; E70544.
DR   AlphaFoldDB; P9WMM4; -.
DR   SMR; P9WMM4; -.
DR   EnsemblBacteria; AAK45907; AAK45907; MT1639.
DR   KEGG; mtc:MT1639; -.
DR   HOGENOM; CLU_048577_1_1_11; -.
DR   UniPathway; UPA00031; UER00009.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR010188; HisA/PriA_Actinobacteria.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR43090; PTHR43090; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01919; hisA-trpF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Histidine biosynthesis; Isomerase; Tryptophan biosynthesis.
FT   CHAIN           1..244
FT                   /note="Phosphoribosyl isomerase A"
FT                   /id="PRO_0000427278"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  25632 MW;  8B9C2C403958A01E CRC64;
     MPLILLPAVD VVEGRAVRLV QGKAGSQTEY GSAVDAALGW QRDGAEWIHL VDLDAAFGRG
     SNHELLAEVV GKLDVQVELS GGIRDDESLA AALATGCARV NVGTAALENP QWCARVIGEH
     GDQVAVGLDV QIIDGEHRLR GRGWETDGGD LWDVLERLDS EGCSRFVVTD ITKDGTLGGP
     NLDLLAGVAD RTDAPVIASG GVSSLDDLRA IATLTHRGVE GAIVGKALYA RRFTLPQALA
     AVRD