P50909 (TRPB1_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan synthase beta chain 1
EC=4.2.1.20

Gene names

Name:	trpB1
Synonyms:	trpB
Ordered Locus Names:	TM_0138

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. HAMAP MF_00133
Catalytic activity	L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O. HAMAP MF_00133
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_00133
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP MF_00133
Subunit structure	Tetramer of two alpha and two beta chains By similarity.
Sequence similarities	Belongs to the TrpB family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro tryptophan synthase 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 – 389	389	Tryptophan synthase beta chain 1 HAMAP MF_00133		PRO_0000099013
Amino acid modifications
	Modified residue	83	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50909 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 23AF62465A3E1CDE	FASTA	389	42,917
	10 20 30 40 50 60 MKGYFGPYGG QYVPEILMPA LEELEAAYEE IMKDESFWKE FNDLLRDYAG RPTPLYFARR 70 80 90 100 110 120 LSEKYGARIY LKREDLLHTG AHKINNAIGQ VLLAKKMGKT RIIAETGAGQ HGVATATAAA 130 140 150 160 170 180 LFGMECVIYM GEEDTIRQKP NVERMKLLGA KVVPVKSGSR TLKDAINEAL RDWITNLQTT 190 200 210 220 230 240 YYVIGSVVGP HPYPIIVRNF QKVIGEETKK QILEKEGRLP DYIVACVGGG SNAAGIFYPF 250 260 270 280 290 300 IDSGVKLIGV EAGGEGLETG KHAASLLKGK IGYLHGSKTF VLQDDWGQVQ VTHSVSAGLD 310 320 330 340 350 360 YSGVGPEHAY WRETGKVLYD AVTDEEALDA FIELSRLEGI IPALESSHAL AYLKKINIKG 370 380 KVVVVNLSGR GDKDLESVLN HPYVRERIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima." Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K. EMBO J. 14:4395-4402(1995) [PubMed: 7556082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X92729 Genomic DNA. Translation: CAA63391.1. AE000512 Genomic DNA. Translation: AAD35231.1.
PIR	S59049.
RefSeq	NP_227953.1. NC_000853.1.
3D structure databases
ProteinModelPortal	P50909.
SMR	P50909. Positions 4-379.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	896968.
GenomeReviews	Gene locus TM_0138 in contig AE000512_GR.
KEGG	tma:TM0138.
NMPDR	fig|243274.1.peg.137.
PATRIC	23935118. VBITheMar51294_0137.
TIGR	TM_0138.
Phylogenomic databases
HOGENOM	HBG303148.
OMA	LKREDLC.
PhylomeDB	P50909.
ProtClustDB	PRK04346.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-345. TMAR243274:TM_0138-MONOMER.
Family and domain databases
HAMAP	MF_00133. Trp_synth_beta. [Tree]
InterPro	IPR001926. PyrdxlP-dep_enz_bsu. IPR006653. Trp_synth_b_CS. IPR006654. Trp_synth_beta. IPR023026. Trp_synth_beta/beta-like. [Graphical view]
KO	K01696.
PANTHER	PTHR10314:SF3. PTHR10314:SF3. 1 hit.
Pfam	PF00291. PALP. 1 hit. [Graphical view]
PIRSF	PIRSF001413. Trp_syn_beta. 1 hit.
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR00263. TrpB. 1 hit.
PROSITE	PS00168. TRP_SYNTHASE_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPB1_THEMA

Accession

Primary (citable) accession number: P50909

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program