ID   TRPC_HELPJ              Reviewed;         452 AA.
AC   Q9ZJU8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Tryptophan biosynthesis protein TrpCF;
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase;
DE              Short=IGPS;
DE              EC=4.1.1.48;
DE   Includes:
DE     RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase;
DE              Short=PRAI;
DE              EC=5.3.1.24;
GN   Name=trpC; OrderedLocusNames=jhp_1200;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC       tryptophan biosynthetic pathway. The first reaction is catalyzed by the
CC       isomerase, coded by the TrpF domain; the second reaction is catalyzed
CC       by the synthase, coded by the TrpC domain (By similarity).
CC       {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC       {ECO:0000305}.
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; AE001439; AAD06779.1; -; Genomic_DNA.
DR   PIR; D71836; D71836.
DR   RefSeq; WP_001141390.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJU8; -.
DR   SMR; Q9ZJU8; -.
DR   STRING; 85963.jhp_1200; -.
DR   EnsemblBacteria; AAD06779; AAD06779; jhp_1200.
DR   KEGG; hpj:jhp_1200; -.
DR   PATRIC; fig|85963.30.peg.1372; -.
DR   eggNOG; COG0134; Bacteria.
DR   eggNOG; COG0135; Bacteria.
DR   OMA; YDIIGIN; -.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00331; IGPS; 1.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.20.20.70; -; 2.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854; PTHR22854; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   SUPFAM; SSF51366; SSF51366; 2.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Isomerase; Lyase; Multifunctional enzyme; Tryptophan biosynthesis.
FT   CHAIN           1..452
FT                   /note="Tryptophan biosynthesis protein TrpCF"
FT                   /id="PRO_0000154281"
FT   REGION          1..253
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          254..448
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
SQ   SEQUENCE   452 AA;  50678 MW;  153AD3B136C632F0 CRC64;
     MPSVLENILK DKLLEVAVLK KNHALPINIA PSDRDFKKAL LEKKTSFILE YKKASPSKGL
     IRKDFDLLEI TKTYEKFASC VSVLADSKYF LGSYENIKIV SQHSTKPILC KDFIIDAFQI
     KLARVMGSNA VLLMLSVLDD KNYLELFNLA KSLNMSVLTE VSNQQEIERL LKLQYDIIGI
     NNRDLHTLKT DIFHTLELRP LLPKDAIIIS ESGIYSHAQI KALAPCVNGF LVGSSLMKEK
     DLKKACIKLI LGENKVCGLT RIKDAKAVYK NHFIYGGLIF EKSSPRYIKP KEALKITKAV
     KKLDFVGVFV KDKIKKIAKI AKKLDLKAVQ LYGYSQKEIA QLKKSLPKTC AIWQVVSVAD
     SKDLAPKTKE ASLILYDTKG DKMGGNGVSF DWEILENAKT PFMLAGGLNL DNIQKALKIK
     ALGLDFNSGL EISPGIKNKD KIKQLARILR EY