HIS4_MYCPA
ID HIS4_MYCPA Reviewed; 243 AA.
AC P60583;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=MAP_1297;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03614.1; -; Genomic_DNA.
DR RefSeq; WP_003876209.1; NC_002944.2.
DR AlphaFoldDB; P60583; -.
DR SMR; P60583; -.
DR STRING; 262316.MAP_1297; -.
DR EnsemblBacteria; AAS03614; AAS03614; MAP_1297.
DR KEGG; mpa:MAP_1297; -.
DR PATRIC; fig|262316.17.peg.1366; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000580; 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; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..243
FT /note="Phosphoribosyl isomerase A"
FT /id="PRO_0000142084"
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; 25402 MW; 9CEF291A709246CE CRC64;
MLILLPAVDV VDGRAVRLVQ GKAGSETEYG SALDAALGWQ RDGAEWIHLV DLDAAFGRGS
NRELLAEVVG KLDVRVELSG GIRDDDSLAA ALATGCARVN LGTAALENPQ WCARAIGEHG
DKVAVGLDVQ IIDGQHRLRG RGWETDGGDL WEVLERLERQ GCSRYVVTDV TKDGTLGGPN
LDLLGAVADR TDAPVIASGG VSSLDDLRAI ATLTGRGVEG AIVGKALYAG RFTLPQALAA
VAE
