HIS4_MYCUA
ID HIS4_MYCUA Reviewed; 244 AA.
AC A0PP18;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=MUL_1576;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL04087.1; -; Genomic_DNA.
DR RefSeq; WP_011739707.1; NC_008611.1.
DR AlphaFoldDB; A0PP18; -.
DR SMR; A0PP18; -.
DR STRING; 362242.MUL_1576; -.
DR EnsemblBacteria; ABL04087; ABL04087; MUL_1576.
DR KEGG; mul:MUL_1576; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000765; 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_0000290569"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 244 AA; 25432 MW; 23FF4C7D18B9D9B2 CRC64;
MPLILLPAVD VVEGRAVRLV QGKAGSETEY GSALDAALGW QRDGAEWIHL VDLDAAFGRG
SNRELLAEVV GKLDVAVELS GGIRDDDSLA AALATGCARV NLGTAALENP QWCARMIAEH
GEKVAVGLDV QIVGGKHRLR GRGWETDGGD LWEVLQRLDS EGCSRYVVTD VTKDGTLAGP
NLELLAGVAG RTEAPVIASG GVSSLDDLRA IATLTGQGVE GAIVGKALYA GRFTLPQALT
AVRE
