ID   TRPF_HALLT              Reviewed;         214 AA.
AC   B9LQ97;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE            Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE            EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN   Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; OrderedLocusNames=Hlac_1940;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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_00135};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00135}.
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DR   EMBL; CP001365; ACM57518.1; -; Genomic_DNA.
DR   RefSeq; WP_015910643.1; NC_012029.1.
DR   AlphaFoldDB; B9LQ97; -.
DR   SMR; B9LQ97; -.
DR   STRING; 416348.Hlac_1940; -.
DR   EnsemblBacteria; ACM57518; ACM57518; Hlac_1940.
DR   GeneID; 7399892; -.
DR   KEGG; hla:Hlac_1940; -.
DR   eggNOG; arCOG01983; Archaea.
DR   HOGENOM; CLU_076364_2_1_2; -.
DR   OMA; FYAKSPR; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000740; Chromosome 1.
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; -; 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; PTHR42894; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..214
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_1000197136"
SQ   SEQUENCE   214 AA;  22479 MW;  749EF476582701A7 CRC64;
     MARVKICGLT RGADLRAAID AGADAVGVIS EVPVDSPREV DPATAAELLA DVPPFVTATL
     VTMPDSAERA VELLRTICPD AIQLHGEWTP DEIRFIRAET ERKVLLAVDA DDPARAEEFD
     RVADALVIDS TDDSGAGGTG ETHDWERAGD LADRLTSPVV LAGGLTADNV AEAVRAADPF
     AVDVASGVEL TDGRKDHNAV ARFVANAGRE MELA