Reviewed, UniProtKB/Swiss-Prot O28668 (TRPCD_ARCFU)

Names and origin

Protein names

Recommended name:
    Tryptophan biosynthesis protein trpCD
Including the following 2 domains:
    1- Recommended name:
            Indole-3-glycerol phosphate synthase
                Short name=IGPS
              EC=4.1.1.48
    2- Recommended name:
            Anthranilate phosphoribosyltransferase
              EC=2.4.2.18

Gene names

Name:	trpCD
Ordered Locus Names:	AF_1604

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the second and fourth steps of tryptophan biosynthetic pathway. The second step is catalyzed by the anthranilate phosphoribosyltransferase, coded by the trpD domain and the fourth step is catalyzed by indole-3-glycerol phosphate synthase, coded by the trpC domain. HAMAP MF_00134
Catalytic activity	1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134 N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00134
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. HAMAP MF_00134 Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Sequence similarities	In the N-terminal section; belongs to the trpC family. In the C-terminal section; belongs to the anthranilate phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Glycosyltransferase Lyase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	tryptophan biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	anthranilate phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP indole-3-glycerol-phosphate synthase 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 – 546	546	Tryptophan biosynthesis protein trpCD HAMAP MF_00134		PRO_0000154507
Regions
	Region	1 – 226	226	Indole-3-glycerol phosphate synthase HAMAP MF_00134
	Region	227 – 546	320	Anthranilate phosphoribosyltransferase HAMAP MF_00134

Sequences

	Sequence		Length	Mass (Da)
	O28668-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 289FF9AE07F08D5A	FASTA	546	59,328
	10 20 30 40 50 60 MMDFGFVDSL KGASKRGKNA VIAEVKVRSP IHGDLLRGRR IEDILRAYEK AGAAAISYIT 70 80 90 100 110 120 AEQFSGNFET LKKIVGLTDL PVLRKDFIRG RKEVERTAEV EAAALLLIAR HLKERTAEMV 130 140 150 160 170 180 DFCFEHGIEP LVEVHHAEDL VYAENARAVL INNRDIDRME RDGGSIDVTA KIAEKIRAFK 190 200 210 220 230 240 VSGSGIGSVE DLLFVLQYVD AALIGTAFMM AENTEEFVQT VCGGEKMIED VLRGLDFDKA 250 260 270 280 290 300 YELAKTLPEL DEIKIAAVLA ALEAKGYGAE VIAGFAKGVA EKSKIEIGKV MDTCGTGGDK 310 320 330 340 350 360 TSSINVSTAV AIALSTVHPV AKHGNRAVSS KSGSADVLEA LGVRIEMDEE RARKMIAETN 370 380 390 400 410 420 FAFLFAPLYH KSFARVAAVR RNLGIRTIFN VTGPLTNPAR PEVQIVGVAS EILLVEVAKA 430 440 450 460 470 480 MSLLGRRAVV VYGSGMDEVN PNSSTDIAVV NGGVERLKLE PEDFGIERCR VLPCSSSGES 490 500 510 520 530 540 AERIRAVFSG KGLKEDRRLI AINFATALFA LGYEDLKENV EIFEEKVQSG ELARKLEEIA CKSTSM

References

[1]

"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB89645.1.
PIR	C69450.
RefSeq	NP_070433.1.
3D structure databases
SMR	O28668. Positions 4-227, 227-540.
ModBase	Search...
Genome annotation databases
GeneID	1484830.
GenomeReviews	Gene locus AF_1604 in contig AE000782_GR.
KEGG	afu:AF1604.
NMPDR	fig|224325.1.peg.1594.
TIGR	AF_1604.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_1604-MONOMER.
BRENDA	2.4.2.18. 7576. 4.1.1.48. 7576.
Family and domain databases
HAMAP	MF_00134_A. IGPS_A. Fused. [Tree] MF_00211. TrpD. Fused. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR005940. Ant_phspho_trans. IPR000312. Glycosyl_Trfase_fam3. IPR017459. Glycosyl_Trfase_fam3_N. IPR013798. Indole-3-glycerol_P_synth. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. G3DSA:3.40.1030.10. Glyco_trans_3. 1 hit.
Pfam	PF02885. Glycos_trans_3N. 1 hit. PF00591. Glycos_transf_3. 1 hit. PF00218. IGPS. 1 hit. [Graphical view]
TIGRFAMs	TIGR01245. trpD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TRPCD_ARCFU

Accession

Primary (citable) accession number: O28668

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 78 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)