ID   HIS4_MYCA1              Reviewed;         243 AA.
AC   A0QHH8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=MAV_3183;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000479; ABK65541.1; -; Genomic_DNA.
DR   RefSeq; WP_009977380.1; NC_008595.1.
DR   AlphaFoldDB; A0QHH8; -.
DR   SMR; A0QHH8; -.
DR   EnsemblBacteria; ABK65541; ABK65541; MAV_3183.
DR   KEGG; mav:MAV_3183; -.
DR   HOGENOM; CLU_048577_1_1_11; -.
DR   OMA; EWLHLVD; -.
DR   OrthoDB; 794219at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000001574; 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..243
FT                   /note="Phosphoribosyl isomerase A"
FT                   /id="PRO_0000290564"
FT   ACT_SITE        9
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   243 AA;  25362 MW;  197145D4F4C0E774 CRC64;
     MLILLPAVDV VDGRAVRLVQ GKAGSETEYG SALDAALGWQ RDGAEWIHLV DLDAAFGRGS
     NRELLAEVVG KLDVQVELSG GIRDDDSLAA ALATGCARVN LGTAALENPQ WCARAIGEHG
     DKVAVGLDVQ TIDGQHRLRG RGWETDGGDL WEVLERLERQ GCSRYVVTDV TKDGTLGGPN
     LDLLGAVADR TDAPVIASGG VSSLDDLRAI ATLTGRGVEG AIVGKALYAG RFTLPQALAA
     VAE