Q88ZU5 (SERC_LACPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoserine aminotransferase
EC=2.6.1.52

Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT

Gene names

Name:	serC
Ordered Locus Names:	lp_0204

Organism

Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)

Taxonomic identifier

220668 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP MF_00160
Catalytic activity	O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP MF_00160 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP MF_00160
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_00160
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160
Subunit structure	Homodimer By similarity. HAMAP MF_00160
Subcellular location	Cytoplasm By similarity HAMAP MF_00160.
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Pyridoxine biosynthesis Serine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150177
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	234 – 235	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	100	1	Pyridoxal phosphate By similarity
	Binding site	150	1	Pyridoxal phosphate By similarity
	Binding site	170	1	Pyridoxal phosphate By similarity
	Binding site	193	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	194	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q88ZU5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4DA8759B92DBD700	FASTA	357	38,701
	10 20 30 40 50 60 MPIYNFSAGP AVLPQPVITQ IQAELPSFRD SGMSILEISH RSDLFAQVLQ DAEQDLRDLM 70 80 90 100 110 120 AIPDNYHVLF FQGGGTLQFT AAPLNLAPHH RIGLLDSGHW AQRAADEAKR VGTKVTILGS 130 140 150 160 170 180 SAANHFNQLP TVVQPIDQSL DYIHLTTNNT IEGTMMTRLP VTGQVPLVAD MSSNFLGEPY 190 200 210 220 230 240 QVSDFGLIFA GAQKNLGPAG LTIVIVRDDL IGQVANLPSM LDYQLFAAKD SMFNTPPVFA 250 260 270 280 290 300 IYAAGLVLKW LKAQGGLSTM TARNHAKAAL LYDFLDQSQL FTNPVKTSDR STMNVPFVTG 310 320 330 340 350 QADLDAAVIQ GAREHGLLNL KGHRLVGGMR ASLYNAMPLA GVQALVDYLA AFEAHHR

References

[1]

"Complete genome sequence of Lactobacillus plantarum WCFS1." Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J. Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL935263 Genomic DNA. Translation: CCC77742.1.
RefSeq	NP_784031.1. NC_004567.1.
3D structure databases
ProteinModelPortal	Q88ZU5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1061425.
GenomeReviews	Gene locus lp_0204 in contig AL935263_GR.
KEGG	lpl:lp_0204.
NMPDR	fig|220668.1.peg.165.
PATRIC	22246963. VBILacPla27411_0168.
Phylogenomic databases
HOGENOM	HBG289982.
OMA	YEVLFLQ.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	LPLA220668:LP_0204-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR022278. Pser_aminoTfrase. IPR003248. Pser_aminoTfrase_subgr. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00831.
PANTHER	PTHR21152:SF1. PTHR21152:SF1. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
PIRSF	PIRSF000525. SerC. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01364. SerC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_LACPL

Accession

Primary (citable) accession number: Q88ZU5
Secondary accession number(s): F9UT11

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program