Reviewed, UniProtKB/Swiss-Prot P59459 (TRPC_BUCBP)

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
Ordered Locus Names:	bbp_259

Organism

Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP]

Taxonomic identifier

135842 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	469 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 – 469	469	Tryptophan biosynthesis protein trpCF HAMAP MF_00134		PRO_0000154273
Regions
	Region	1 – 257	257	Indole-3-glycerol phosphate synthase HAMAP MF_00134
	Region	258 – 469	212	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134

Sequences

	Sequence		Length	Mass (Da)
	P59459-1 [UniParc]. Last modified March 28, 2003. Version 1. Checksum: 089802BE9F178FD9	FASTA	469	54,239
	10 20 30 40 50 60 MNSILKEIIN DKLMWVKYHK KKQPLFTFQN KIVRSNYNFK NSLKSIHPSY ILEIKKASPS 70 80 90 100 110 120 LGIINNKLDL KKISLIYKKY ASSISILTDE KYFHGNFEFI PIVRKIAHRQ PILCKDFFID 130 140 150 160 170 180 PYQIYLARYY QADAILLMLS ILNDNQYVFL RNIAEMLNMD VLTEIENKKE LTRAINLKSK 190 200 210 220 230 240 IIGINNRNLN NLSIDIQKTK VLAPLIPKKI IIISESGIQN YNQIRQLKPF VQGFLIGSNL 250 260 270 280 290 300 MRKKNLEEAV CKMILGNNKI CGLTQSSDVK IIKEYGIVYG GLIFCKFSPR YINCNNAYSI 310 320 330 340 350 360 INNVSLKYIG VFCNENLKRV AYIGTKLSLH AVQLHGNEDQ IYINNLKLIL PKHIKIWKSI 370 380 390 400 410 420 IYLDFLKNQK HLFYNVNKYI IDNKDGGSGK TFNWKYLKNC KLDNVILAGG LDINNCILAT 430 440 450 460 DLGCYGYDFN SKLESSPGIK DLKKIVALTY SLRRHTVFNY RNLICLGKK

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016826 Genomic DNA. Translation: AAO26986.1.
RefSeq	NP_777881.1.
3D structure databases
HSSP	HSSP built from PDB template 1JCM based on UniProtKB P00909.
ModBase	Search...
Genome annotation databases
GeneID	1058465.
GenomeReviews	Gene locus bbp_259 in contig AE016826_GR.
KEGG	bab:bbp259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P59459.
OMA	YILECKK.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_259-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_BUCBP

Accession

Primary (citable) accession number: P59459

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	November 3, 2009
This is version 46 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)