ID   HIS4_MYCSJ              Reviewed;         248 AA.
AC   A3Q127;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Phosphoribosyl isomerase A {ECO:0000255|HAMAP-Rule:MF_01014};
DE   AltName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014};
DE   AltName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
DE            Short=PRAI {ECO:0000255|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_01014};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
GN   Name=priA {ECO:0000255|HAMAP-Rule:MF_01014};
GN   Synonyms=hisA {ECO:0000255|HAMAP-Rule:MF_01014};
GN   OrderedLocusNames=Mjls_3075;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in both the histidine and tryptophan biosynthetic
CC       pathways. {ECO:0000255|HAMAP-Rule:MF_01014}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01014};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01014};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01014}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01014}.
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DR   EMBL; CP000580; ABN98854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3Q127; -.
DR   SMR; A3Q127; -.
DR   KEGG; mjl:Mjls_3075; -.
DR   HOGENOM; CLU_048577_1_1_11; -.
DR   BioCyc; MSP164757:G1G8C-3100-MONOMER; -.
DR   UniPathway; UPA00031; UER00009.
DR   UniPathway; UPA00035; UER00042.
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; Aldolase class I; 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   NCBIfam; TIGR01919; hisA-trpF; 1.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Histidine biosynthesis; Isomerase; Tryptophan biosynthesis.
FT   CHAIN           1..248
FT                   /note="Phosphoribosyl isomerase A"
FT                   /id="PRO_0000290566"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   248 AA;  26204 MW;  1A2CBB2F54221470 CRC64;
     MSEKRPLILL PAVDVVEGRA VRLVQGKAGS ETEYGSALDA ALGWQRDGAE WIHLVDLDAA
     FGRGSNRELL ADVVGRLDVA VELSGGIRDD ESLEAALATG CARVNIGTAA LENPQWCAKV
     VAEFGDKVAV GLDVKIVDDQ HRLRGRGWET DGGDLWEVLD RLDSEGCSRY VVTDVTKDGT
     LQGPNLDLLG RVADRTDAPV IASGGVSSLD DLRAIATLTD RGVEGAIVGK ALYAGRFTLP
     EALAAMGQ
//