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Database: UniProt
Entry: D6ZZK1_STAND
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ID   D6ZZK1_STAND            Unreviewed;       236 AA.
AC   D6ZZK1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|ARBA:ARBA00022272, ECO:0000256|HAMAP-Rule:MF_00135};
DE            Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000256|ARBA:ARBA00012572, ECO:0000256|HAMAP-Rule:MF_00135};
GN   Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN   OrderedLocusNames=Snov_3926 {ECO:0000313|EMBL:ADH91196.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS   12100 / NBRC 12443 / NCIMB 10456).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Ancylobacter.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH91196.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|EMBL:ADH91196.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC   12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA   Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA   Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA   Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic and
RT   methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT   8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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         ECO:0000256|HAMAP-Rule:MF_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC       ECO:0000256|HAMAP-Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00135}.
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DR   EMBL; CP002026; ADH91196.1; -; Genomic_DNA.
DR   RefSeq; WP_013168697.1; NC_014217.1.
DR   AlphaFoldDB; D6ZZK1; -.
DR   STRING; 639283.Snov_3926; -.
DR   KEGG; sno:Snov_3926; -.
DR   eggNOG; COG0135; Bacteria.
DR   HOGENOM; CLU_076364_1_1_5; -.
DR   OrthoDB; 9796196at2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
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   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:ADH91196.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT   DOMAIN          5..208
FT                   /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT                   /evidence="ECO:0000259|Pfam:PF00697"
FT   REGION          213..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   236 AA;  24587 MW;  BE8E0C8D5DABB649 CRC64;
     MSLEIKICGL STAETLDTAL GAGADMVGMV FFPPSPRHVD LSTAGALAAK ARGRARIVAL
     TVDADDVALA DIVAAIHPDM LQLHGKESPE RVAAIRARFE LPVMKAVGIA TAADLAALTA
     YERVADRLLL DAKPPKDAVL PGGNGVPFDW DLLAGLDLSI PYMLSGGLDP ENVREAVQRL
     HPFGVDVSSG VERAPGVKDI ARIVAFIREA RAADPSNPST GGKPAQPSSA RETSLS
//
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