ID   TRPF_METTM              Reviewed;         226 AA.
AC   P26941; D9PUE8;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=trpF; OrderedLocusNames=MTBMA_c02370;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=1860817; DOI=10.1128/jb.173.16.5017-5023.1991;
RA   Meile L., Stettler R., Banholzer R., Kotik M., Leisinger T.;
RT   "Tryptophan gene cluster of Methanobacterium thermoautotrophicum Marburg:
RT   molecular cloning and nucleotide sequence of a putative trpEGCFBAD
RT   operon.";
RL   J. Bacteriol. 173:5017-5023(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADL57846.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M65060; AAA73031.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL57846.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P26941; -.
DR   SMR; P26941; -.
DR   STRING; 79929.MTBMA_c02370; -.
DR   PaxDb; 79929-MTBMA_c02370; -.
DR   KEGG; mmg:MTBMA_c02370; -.
DR   PATRIC; fig|79929.8.peg.233; -.
DR   HOGENOM; CLU_076364_2_0_2; -.
DR   UniPathway; UPA00035; UER00042.
DR   Proteomes; UP000000345; 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; Aromatic amino acid biosynthesis; Isomerase;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..226
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154408"
SQ   SEQUENCE   226 AA;  24383 MW;  CDE5A34BF155E034 CRC64;
     MKIKICGLTR EEDVVLADSL GADLLGFIHA RRSPRHLELG DVAELSSLIP DEKAVLVTET
     SETSRIMEAI DKTGIERIQL HSVSPETAGK IHESLHAEGY SLELTLAVPP LSSHICGHEF
     QGISGLILDS ASGGRTGGTG KIIPPSDALE LLALIRGMDP SLRVTLAGGL TLEFVRKNRE
     YVSKFDCLDF NSGIETGPGV KDHEMMAELM NYIEGLPTRK GAIEEI
//