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P22098

- TRPC_VIBPA

UniProt

P22098 - TRPC_VIBPA

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Protein

Tryptophan biosynthesis protein TrpCF

Gene

trpC

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity).By similarity

Catalytic activityi

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.

Pathwayi

GO - Molecular functioni

  1. indole-3-glycerol-phosphate synthase activity Source: UniProtKB-EC
  2. phosphoribosylanthranilate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. tryptophan biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciVPAR223926:GHK4-2014-MONOMER.
UniPathwayiUPA00035; UER00042.
UPA00035; UER00043.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan biosynthesis protein TrpCF
Including the following 2 domains:
Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
Short name:
IGPS
N-(5'-phospho-ribosyl)anthranilate isomerase (EC:5.3.1.24)
Short name:
PRAI
Gene namesi
Name:trpC
Synonyms:trpC-TRPF
Ordered Locus Names:VP1959
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002493: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Tryptophan biosynthesis protein TrpCFPRO_0000154286Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi223926.VP1959.

Structurei

3D structure databases

ProteinModelPortaliP22098.
SMRiP22098. Positions 25-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 283283Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni284 – 481198N-(5'-phosphoribosyl)anthranilate isomeraseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the TrpC family.Curated
In the C-terminal section; belongs to the TrpF family.Curated

Phylogenomic databases

eggNOGiCOG0134.
HOGENOMiHOG000280458.
KOiK13498.
OMAiEKYFQGD.
OrthoDBiEOG6WT8JX.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
HAMAPiMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProiIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 2 hits.
PROSITEiPS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22098 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MKMTDFNTQQ ANNLSEHVSK KEAEMAEVLA KIVRDKYQWV AERKASQHLS
60 70 80 90 100
TFQSDLLPSD RSFYDALSGD KTVFITECKK ASPSKGLIRN DFDLDYIASV
110 120 130 140 150
YNNYADAISV LTDEKYFQGS FDFLPQVRRQ VKQPVLCKDF MVDTYQVYLA
160 170 180 190 200
RHYGADAVLL MLSVLNDEEY KALEEAAHSL NMGILTEVSN EEELHRAVQL
210 220 230 240 250
GARVIGINNR NLRDLTTDLN RTKALAPTIR KLAPNATVIS ESGIYTHQQV
260 270 280 290 300
RDLAEYADGF LIGSSLMAED NLELAVRKVT LGENKVCGLT HPDDAAKAYQ
310 320 330 340 350
AGAVFGGLIF VEKSKRAVDF ESARLTMSGA PLNYVGVFQN HDVDYVASIV
360 370 380 390 400
TSLGLKAVQL HGLEDQEYVN QLKTELPVGV EIWKAYGVAD TKPSLLADNI
410 420 430 440 450
DRHLLDAQVG TQTGGTGHVF DWSLIGDPSQ IMLAGGLSPE NAQQAAKLGC
460 470 480
LGLDLNSGVE SAPGKKDSQK LQAAFHAIRN Y
Length:481
Mass (Da):52,974
Last modified:April 4, 2003 - v2
Checksum:iBC575AD8FB57FC00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031R → K in CAA35034. (PubMed:1773058)Curated
Sequence conflicti449 – 4491G → A in CAA35034. (PubMed:1773058)Curated
Sequence conflicti476 – 4761H → R in CAA35034. (PubMed:1773058)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17149 Genomic DNA. Translation: CAA35034.1.
BA000031 Genomic DNA. Translation: BAC60222.1.
RefSeqiNP_798338.1. NC_004603.1.

Genome annotation databases

EnsemblBacteriaiBAC60222; BAC60222; BAC60222.
GeneIDi1189470.
KEGGivpa:VP1959.
PATRICi20142086. VBIVibPar50997_1874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17149 Genomic DNA. Translation: CAA35034.1 .
BA000031 Genomic DNA. Translation: BAC60222.1 .
RefSeqi NP_798338.1. NC_004603.1.

3D structure databases

ProteinModelPortali P22098.
SMRi P22098. Positions 25-286.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 223926.VP1959.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC60222 ; BAC60222 ; BAC60222 .
GeneIDi 1189470.
KEGGi vpa:VP1959.
PATRICi 20142086. VBIVibPar50997_1874.

Phylogenomic databases

eggNOGi COG0134.
HOGENOMi HOG000280458.
KOi K13498.
OMAi EKYFQGD.
OrthoDBi EOG6WT8JX.

Enzyme and pathway databases

UniPathwayi UPA00035 ; UER00042 .
UPA00035 ; UER00043 .
BioCyci VPAR223926:GHK4-2014-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
HAMAPi MF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProi IPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 2 hits.
PROSITEi PS00614. IGPS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and features of the tryptophan operon of Vibrio parahemolyticus."
    Crawford I.P., Han C.Y., Silverman M.
    DNA Seq. 1:189-196(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BB22.
  2. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
    Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
    Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIMD 2210633.

Entry informationi

Entry nameiTRPC_VIBPA
AccessioniPrimary (citable) accession number: P22098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 4, 2003
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3