P59459 (TRPC_BUCBP) 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:	bbp_259

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	469 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. HAMAP MF_00134_B
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP MF_00134_B 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134_B
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP MF_00134_B Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer By similarity. HAMAP 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-KW
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 – 469	469	Tryptophan biosynthesis protein TrpCF HAMAP MF_00134_B		PRO_0000154273
Regions
	Region	1 – 257	257	Indole-3-glycerol phosphate synthase HAMAP MF_00134_B
	Region	258 – 469	212	N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134_B

Sequences

	Sequence		Length	Mass (Da)
	P59459 [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]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26986.1.
RefSeq	NP_777881.1. NC_004545.1.
3D structure databases
ProteinModelPortal	P59459.
SMR	P59459. Positions 1-260.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002317; EBBUCP00000002141; EBBUCG00000002317.
GeneID	1058465.
GenomeReviews	Gene locus bbp_259 in contig AE016826_GR.
KEGG	bab:bbp259.
PATRIC	21245299. VBIBucAph80364_0252.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008187.
HOGENOM	HBG296890.
OMA	YILECKK.
PhylomeDB	P59459.
ProtClustDB	PRK09427.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_259-MONOMER.
Family and domain databases
HAMAP	MF_00134_B. IGPS_B. Fused. [Tree] MF_00135. PRAI. Fused. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GlycerolPSynthase_CS. IPR001240. PRAI. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
KO	K13498.
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_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:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program