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Database: UniProt
Entry: A0A2A4VQ51_9PROT
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Original site: A0A2A4VQ51_9PROT 
ID   A0A2A4VQ51_9PROT        Unreviewed;       171 AA.
AC   A0A2A4VQ51;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272};
DE            EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572};
DE   Flags: Fragment;
GN   ORFNames=COB37_10115 {ECO:0000313|EMBL:PCI60193.1};
OS   Kordiimonadales bacterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX   NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI60193.1, ECO:0000313|Proteomes:UP000217879};
RN   [1] {ECO:0000313|Proteomes:UP000217879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001164};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCI60193.1}.
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DR   EMBL; NVTU01000041; PCI60193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4VQ51; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000217879; Unassembled WGS sequence.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR044643; TrpF_fam.
DR   PANTHER; PTHR42894; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR   PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:PCI60193.1}.
FT   DOMAIN          5..171
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
FT   NON_TER         171
FT                   /evidence="ECO:0000313|EMBL:PCI60193.1"
SQ   SEQUENCE   171 AA;  18278 MW;  5EFD9BF04A461081 CRC64;
     MAVDVKICGI TEAEHAHFAA EHGARWLGFV FFEKSPRNLS LEAAEALGKI LPTGPKRVGV
     FVNASDTLLK AAIAALSLDA VQLHGDETPA DAKRLKELLG VKIIKAVAIS NEDDITKADP
     FLPHVDRILF DAKPPKGAVL PGGNAVSFPW HILKGKGLPY RWMLAGGLTA E
//
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