P00910 (TRPC_SALTY) 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
Ordered Locus Names:	STM1725

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	452 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 Reference proteome
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 – 452	452	Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B		PRO_0000154284
Regions
	Region	1 – 256	256	Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
	Region	257 – 452	196	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

	Sequence		Length	Mass (Da)
	P00910 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: AF0DC781A2F75859	FASTA	452	49,202
	10 20 30 40 50 60 MQTVLAKIVA DKAIWVEARK QQQPLASFQN EIQPSTRHFY DALQGARTAF ILECKKASPS 70 80 90 100 110 120 KGVIRDDFDP ARIASIYQHY ASAISVLTDE KYFQGSFDFL PVVSQSAPQP ILCKDFIIDP 130 140 150 160 170 180 YQIYLARYYQ ADACLLMLSV LDDEQYRQLS AVAHSLKMGV LTEVSNDEER ERAIALGAKV 190 200 210 220 230 240 VGINNRDLRD LSIDLNRTRQ LAPKLGHGVT VISESGINTY GQVRELSHFA NGFLIGSALM 250 260 270 280 290 300 AHDDLNAAVR RVLLGENKVC GLTRAQDAKA ACDAGAIYGG LIFVPSSPRA VSVEQAREVI 310 320 330 340 350 360 SGAPLQYVGV FKNADIADVC QKAAVLSLSA VQLHGSEDQA YVNALREALP KQVQIWKALS 370 380 390 400 410 420 VSDALPARDY HHVDKYIFDN GQGGSGQRFD WSLLQGQPLD NVLLAGGLAA DNCVQAAQVG 430 440 450 CAGLDFNSGV ESQPGIKDAR LLASVFQTLR AY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium." Horowitz H., van Arsdell J., Platt T. J. Mol. Biol. 169:775-797(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M30286 Genomic DNA. Translation: AAA27237.1. AE006468 Genomic DNA. Translation: AAL20643.1.
PIR	GWEBT. A01132.
RefSeq	NP_460684.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P00910.
SMR	P00910. Positions 1-452.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM1725.
Proteomic databases
PaxDb	P00910.
PRIDE	P00910.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL20643; AAL20643; STM1725.
GeneID	1253244.
KEGG	stm:STM1725.
PATRIC	32381963. VBISalEnt20916_1821.
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_SALTY

Accession

Primary (citable) accession number: P00910

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program