P42393 (TRPC_BUCAP) 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/F
Ordered Locus Names:	BUsg_268

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	451 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 By similarity. HAMAP-Rule MF_00134_B
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 – 451	451	Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B		PRO_0000154272
Regions
	Region	1 – 256	256	Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
	Region	257 – 451	195	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sequences

	Sequence		Length	Mass (Da)
	P42393 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 88FD5F0E84FA7B71	FASTA	451	51,594
	10 20 30 40 50 60 MQETILNKII KDKIDWIKYR KKIQPLIKFK NKINKETRNF YNSLKEKRPF FILECKKSSP 70 80 90 100 110 120 SLGIIRKKFN LIEIANIYKN YASAISVLTD EKYFHGNIEY INVVRRCVSQ PILCKDFFID 130 140 150 160 170 180 SYQVYLARYY SADAILLMLS VLNDSQYLEL SRIAKELNMG VLTEINNIKE LKRAIKLNAS 190 200 210 220 230 240 VIGINNRNLH DLSIDLNRTR TLSPLIKNKI IVSESGIKKN HQIKELSNIV HGFLIGSSLM 250 260 270 280 290 300 YRTNLETNIK SLIIGDNKVC GLTRIIDAKI VESCGAVYGG LIFADNSLRK TNEKIAEKMI 310 320 330 340 350 360 FENNLRFIGV FQNQDIEKIV NIAQRLSLYA VQLHGSENQK YINILRKKLC KKIKIWKAFS 370 380 390 400 410 420 IQSTLPLLNW DHIDKYIFDS GSGGTNKTFN WSILKGSILE NVILAGGINT DNVLIASQLN 430 440 450 CSGLDFNSGV EKSPGIKDHK KISLIFKKLT F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum)." Munson M.A., Baumann P. J. Bacteriol. 175:6426-6432(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19055 Genomic DNA. Translation: CAA79499.1. AE013218 Genomic DNA. Translation: AAM67826.1.
PIR	B49897.
RefSeq	NP_660615.1. NC_004061.1.
3D structure databases
ProteinModelPortal	P42393.
SMR	P42393. Positions 3-259.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67826; AAM67826; BUsg_268.
GeneID	1005470.
KEGG	bas:BUsg268.
PATRIC	21247341. VBIBucAph100086_0280.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0134.
KO	K13498.
OMA	YILECKK.
ProtClustDB	PRK09427.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-282-MONOMER.
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_dom. 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_BUCAP

Accession

Primary (citable) accession number: P42393

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program