TRPF_ZYMMT
ID TRPF_ZYMMT Reviewed; 211 AA.
AC Q9S3U4; F8ERS7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=Zymop_0633;
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 / NCIMB
RC 11200 / NRRL B-4491 / Barker I;
RA Eddy C.K., Ingram L.O.;
RT "Zymomonas trpFBA genes.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 / NCIMB
RC 11200 / NRRL B-4491 / Barker I;
RX PubMed=21742897; DOI=10.1128/jb.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF173835; AAD51337.1; -; Genomic_DNA.
DR EMBL; CP002865; AEI37535.1; -; Genomic_DNA.
DR RefSeq; WP_013933934.1; NC_015709.1.
DR AlphaFoldDB; Q9S3U4; -.
DR SMR; Q9S3U4; -.
DR STRING; 579138.Zymop_0633; -.
DR EnsemblBacteria; AEI37535; AEI37535; Zymop_0633.
DR KEGG; zmp:Zymop_0633; -.
DR PATRIC; fig|579138.3.peg.666; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_1_1_5; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000491; 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; -; 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..211
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_0000154396"
FT CONFLICT 10
FT /note="I -> L (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..26
FT /note="PETLLAAVKNGASH -> EETVETAVRYGADY (in Ref. 1;
FT AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..45
FT /note="AVQPEMAS -> SVTPEKAA (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="NR -> RQ (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="ID -> VQ (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="L -> F (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="D -> N (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..75
FT /note="VVHA -> ALAS (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="P -> A (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..96
FT /note="VAFIRR -> IASIRE (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..111
FT /note="PITR -> SIAN (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..119
FT /note="DQTL -> AQAP (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="V -> A (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> L (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> V (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="K -> R (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..159
FT /note="DYNHPMA -> EYKHPLP (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="D -> H (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="V -> I (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> S (in Ref. 1; AAD51337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23262 MW; 385307A59D1F856E CRC64;
MSVRTKICGI STPETLLAAV KNGASHIGFV FFEKSPRAVQ PEMASMLINR IPDHIDKIGV
LVDPDDNLLE RVVHAGLTGF QLHGHETPER VAFIRRTFPK VKIWKALPIT RSQDLDQTLH
YRGLVDRVLY DARTDGALPG GMGKRFDWRL LKDYNHPMAW ALSGGLDADN IAQAVAITGA
ELVDVSSGVE TAPGIKDMDK IAQFLQAVRL L
