Reviewed, UniProtKB/Swiss-Prot P42393 (TRPC_BUCAP)

Names and origin

Protein names

Recommended name:
    Tryptophan biosynthesis protein trpCF
Including the following 2 domains:
    1- Recommended name:
            Indole-3-glycerol phosphate synthase
                Short name=IGPS
              EC=4.1.1.48
    2- Recommended name:
            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 [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. HAMAP MF_00134
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP MF_00134 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP MF_00134 Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer By similarity.
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: HAMAP
Molecular function	indole-3-glycerol-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: HAMAP
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 MF_00134		PRO_0000154272
Regions
	Region	1 – 256	256	Indole-3-glycerol phosphate synthase HAMAP MF_00134
	Region	257 – 451	195	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Sequences

	Sequence		Length	Mass (Da)
	P42393-1 [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: 8407819] [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: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z19055 Genomic DNA. Translation: CAA79499.1. AE013218 Genomic DNA. Translation: AAM67826.1.
PIR	B49897.
RefSeq	NP_660615.1.
3D structure databases
HSSP	HSSP built from PDB template 1JCM based on UniProtKB P00909.
ModBase	Search...
Genome annotation databases
GeneID	1005470.
GenomeReviews	Gene locus BUsg_268 in contig AE013218_GR.
KEGG	bas:BUsg268.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P42393.
OMA	YILECKK.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG268-MON.
Family and domain databases
HAMAP	MF_00134. Fused. [Tree] MF_00135. Fused. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GPS_central. IPR001240. PRAI. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
ProDom	PD001511. IGPS. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)