P22098 (TRPC_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

1. Indole-3-glycerol phosphate synthase
   Short name=IGPS
   EC=4.1.1.48
2. N-(5'-phospho-ribosyl)anthranilate isomerase
   Short name=PRAI
   EC=5.3.1.24

Gene names

Name:	trpC
Synonyms:	trpC-TRPF
Ordered Locus Names:	VP1959

Organism

Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]

Taxonomic identifier

223926 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio harveyi group › Vibrio parahaemolyticus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. HAMAP-Rule MF_00134_B
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer.
Sequence similarities	In the N-terminal section; belongs to the TrpC family. In the C-terminal section; belongs to the TrpF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Isomerase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	indole-3-glycerol-phosphate synthase activity Inferred from electronic annotation. Source: EC phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B		PRO_0000154286
Regions
	Region	1 – 283	283	Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
	Region	284 – 481	198	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B
Experimental info
	Sequence conflict	203	1	R → K in CAA35034. Ref.1
	Sequence conflict	449	1	G → A in CAA35034. Ref.1
	Sequence conflict	476	1	H → R in CAA35034. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22098 [UniParc]. Last modified April 4, 2003. Version 2. Checksum: BC575AD8FB57FC00	FASTA	481	52,974
	10 20 30 40 50 60 MKMTDFNTQQ ANNLSEHVSK KEAEMAEVLA KIVRDKYQWV AERKASQHLS TFQSDLLPSD 70 80 90 100 110 120 RSFYDALSGD KTVFITECKK ASPSKGLIRN DFDLDYIASV YNNYADAISV LTDEKYFQGS 130 140 150 160 170 180 FDFLPQVRRQ VKQPVLCKDF MVDTYQVYLA RHYGADAVLL MLSVLNDEEY KALEEAAHSL 190 200 210 220 230 240 NMGILTEVSN EEELHRAVQL GARVIGINNR NLRDLTTDLN RTKALAPTIR KLAPNATVIS 250 260 270 280 290 300 ESGIYTHQQV RDLAEYADGF LIGSSLMAED NLELAVRKVT LGENKVCGLT HPDDAAKAYQ 310 320 330 340 350 360 AGAVFGGLIF VEKSKRAVDF ESARLTMSGA PLNYVGVFQN HDVDYVASIV TSLGLKAVQL 370 380 390 400 410 420 HGLEDQEYVN QLKTELPVGV EIWKAYGVAD TKPSLLADNI DRHLLDAQVG TQTGGTGHVF 430 440 450 460 470 480 DWSLIGDPSQ IMLAGGLSPE NAQQAAKLGC LGLDLNSGVE SAPGKKDSQK LQAAFHAIRN Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17149 Genomic DNA. Translation: CAA35034.1. BA000031 Genomic DNA. Translation: BAC60222.1.
RefSeq	NP_798338.1. NC_004603.1.
3D structure databases
ProteinModelPortal	P22098.
SMR	P22098. Positions 25-286.
ModBase	Search...
Protein-protein interaction databases
STRING	223926.VP1959.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC60222; BAC60222; BAC60222.
GeneID	1189470.
KEGG	vpa:VP1959.
PATRIC	20142086. VBIVibPar50997_1874.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0134.
HOGENOM	HOG000280458.
KO	K13498.
OMA	YILECKK.
ProtClustDB	PRK09427.
Enzyme and pathway databases
UniPathway	UPA00035; UER00042. UPA00035; UER00043.
Family and domain databases
Gene3D	3.20.20.70. 2 hits.
HAMAP	MF_00134_B. IGPS_B. Fused. MF_00135. PRAI. Fused.
InterPro	IPR013785. Aldolase_TIM. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GlycerolPSynthase_CS. IPR001240. PRAI. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Pfam	PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 2 hits.
PROSITE	PS00614. IGPS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPC_VIBPA

Accession

Primary (citable) accession number: P22098

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	April 4, 2003
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program