ID J0RLD3_HELPX Unreviewed; 452 AA.
AC J0RLD3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00134, ECO:0000256|HAMAP-Rule:MF_00135};
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
DE Includes:
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN Synonyms=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=HPHPP4D_0934 {ECO:0000313|EMBL:EJC23886.1};
OS Helicobacter pylori Hp P-4d.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992103 {ECO:0000313|EMBL:EJC23886.1, ECO:0000313|Proteomes:UP000004286};
RN [1] {ECO:0000313|EMBL:EJC23886.1, ECO:0000313|Proteomes:UP000004286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-4d {ECO:0000313|EMBL:EJC23886.1,
RC ECO:0000313|Proteomes:UP000004286};
RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT "Genome sequence of Helicobacter pylori Hp P-4d.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025592}.
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 Evidence={ECO:0000256|ARBA:ARBA00001633, ECO:0000256|HAMAP-
CC Rule:MF_00134};
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|HAMAP-Rule:MF_00134}.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC Rule:MF_00134}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|HAMAP-
CC Rule:MF_00135}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family.
CC {ECO:0000256|ARBA:ARBA00009847}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family.
CC {ECO:0000256|ARBA:ARBA00007902}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJC23886.1}.
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DR EMBL; AKQE01000002; EJC23886.1; -; Genomic_DNA.
DR RefSeq; WP_001141469.1; NZ_AKQE01000002.1.
DR AlphaFoldDB; J0RLD3; -.
DR PATRIC; fig|992103.3.peg.914; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000004286; Unassembled WGS sequence.
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; Aldolase class I; 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:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00134};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00134};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00134}; Isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00134}.
FT DOMAIN 5..247
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 254..445
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 452 AA; 50645 MW; 8CCBDE8C96F91274 CRC64;
MPSVLENILK DKLLEVSMLK KNHTLPANIT PSDRDFKKAL LEKKTSFILE CKKASPSKGL
IRKDFDLLEI TKTYEKFASC VSVLADAKHF LGSYENIKII SQHSTKPILC KDFIIDAFQI
KLARVMGSNA VLLMLSVLDD KNYLELFNLA KSLNMSVLTE VSNQQEIERL LKLQYDIIGI
NNRDLHTLKT DIFHTLELRP LLPKDAIIIS ESGIHSHAQI KALAPYVNGF LVGSSLMKEK
DLKKACIKLI LGENKVCGLT RIKDAKAVYK NHFIYGGLIF EKSSPRYIKP KEALKITKAV
KKLDFVGVFV KDSVKKIQKI AKKLDLKAVQ LYGYSPKKIA QLKKSLPKTC AIWQVVSVMN
AKDLTPKAKG ASLILYDTKG DKMGGNGVSF DWEILENAKT PFMLAGGLNL DNIQKALKVK
ALGLDFNSGL EISPGIKNKD KIKRLARILR EY
//
