P54203 (TRPB_PASMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan synthase beta chain
EC=4.2.1.20

Gene names

Name:	trpB
Ordered Locus Names:	PM0578

Organism

Pasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]

Taxonomic identifier

272843 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella

Protein attributes

Sequence length	402 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
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 – 402	402	Tryptophan synthase beta chain HAMAP MF_00133		PRO_0000098976
Amino acid modifications
	Modified residue	88	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	120	1	T → TT in AAC43609. Ref.1
	Sequence conflict	324	1	Q → E in AAC43609. Ref.1
	Sequence conflict	338	1	Q → E in AAC43609. Ref.1
	Sequence conflict	343	1	H → D in AAC43609. Ref.1
	Sequence conflict	366 – 367	2	QP → HA in AAC43609. Ref.1
	Sequence conflict	399	1	Y → H in AAC43609. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54203 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 1F8F38DFD36A2224	FASTA	402	43,624
	10 20 30 40 50 60 MSETLLNPYF GEFGGMYVPE ILMPVLKNLE KAFVEAQQDP TFKETFLDLL KNYAGRPTAL 70 80 90 100 110 120 TRCRNLTQGS KTKLYLKRED LLHGGAHKTN QVLGQILLAK RMGKTRIIAE TGAGQHGVAT 130 140 150 160 170 180 ALACAMLGMP CQIYMGAKDV ERQSPNVFRM RLMGANVTAV TKGSASLKDA CCEAMRDWAE 190 200 210 220 230 240 NYEHTHYLLG TAAGPHPFPT IVREFQKIIG EETKQQILAR EGRLPDAVIA AVGGGSNAIG 250 260 270 280 290 300 MFNDFIEETS VRLIGVEPAG KGIATGQHGA PLGHGTTGIY FGMKAPLMQT PDGQIEESYS 310 320 330 340 350 360 ISAGLDFPSV GPQHAHLQAI GRAQYESITD DEALSAFQAL ARHEGIIPAL ESAHALAYAL 370 380 390 400 KLIQRQPEKE QLLVVNLSGR GDKDIFTVDR ILSQKGVSYA PF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of Pasteurella multocida tryptophan synthase beta-subunit by antisera against strain P1059." Jablonski P.E., Jablonski L.M., Pintado O., Sriranganathan N., Hovde C.J. Microbiology 142:115-121(1996) [PubMed: 8581158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15742 / P1059.
[2]	"Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U22344 Genomic DNA. Translation: AAC43609.1. AE004439 Genomic DNA. Translation: AAK02662.1.
RefSeq	NP_245515.1. NC_002663.1.
3D structure databases
ProteinModelPortal	P54203.
SMR	P54203. Positions 4-392.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1243925.
GenomeReviews	Gene locus PM0578 in contig AE004439_GR.
KEGG	pmu:PM0578.
NMPDR	fig|272843.1.peg.578.
PATRIC	22870338. VBIPasMul88067_0585.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG303148.
OMA	HAASITR.
ProtClustDB	PRK04346.
Enzyme and pathway databases
BioCyc	PMUL272843:PM0578-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

TRPB_PASMU

Accession

Primary (citable) accession number: P54203

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program