Reviewed, UniProtKB/Swiss-Prot A4QCG9 (SERC_CORGB)

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:	cgR_0942

Organism

Corynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]

Taxonomic identifier

340322 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160 Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP MF_00160
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP pyridoxal phosphate binding 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 – 376	376	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058209
Regions
	Region	80 – 81	2	Pyridoxal phosphate binding By similarity
	Region	247 – 248	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	46	1	L-glutamate By similarity
	Binding site	104	1	Pyridoxal phosphate By similarity
	Binding site	150	1	Pyridoxal phosphate By similarity
	Binding site	172	1	Pyridoxal phosphate By similarity
	Binding site	195	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	196	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4QCG9-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 144681484C58D802	FASTA	376	40,050
	10 20 30 40 50 60 MTDFPTLPSE FIPGDGRFGC GPSKVRPEQI QAIVDGSASV IGTSHRQPAV KNVVGSIREG 70 80 90 100 110 120 LSDLFSLPEG YEIILSLGGA TAFWDAATFG LIEKKSGHLS FGEFSSKFAK ASKLAPWLYE 130 140 150 160 170 180 PEIVTAETGD APAPQAFEGA DVIAWAHNET STGAMVPVLR PEGSEGSLVA IDATSGAGGL 190 200 210 220 230 240 PVDIKNSDVY YFSPQKCFAS DGGLWLAAMS PAALERIEKI NASDRFIPEF LNLQTAVDNS 250 260 270 280 290 300 LKNQTYNTPA VATLLMLDNQ VKWMNSNGGL DGMVARTTAS SSALYNWAEA REEASPYVAD 310 320 330 340 350 360 AAKRSLVVGT IDFDDSIDAA VIAKILRANG ILDTEPYRKL GRNQLRIGMF PAIDSTDVEK 370 LTGAIDFILD GGFAKK

References

[1]

"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R." Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M. Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP009044 Genomic DNA. Translation: BAF53916.1.
RefSeq	YP_001137818.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A4QCG9.
Genome annotation databases
GeneID	4992177.
GenomeReviews	Gene locus cgR_0942 in contig AP009044_GR.
KEGG	cgt:cgR_0942.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SAKEETR.
Family and domain databases
HAMAP	MF_00160. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR006272. Ser_trans_bac. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
ProDom	PD001544. Pser_amintransf. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01366. serC_3. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_CORGB

Accession

Primary (citable) accession number: A4QCG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 15, 2007
Last modified:	November 3, 2009
This is version 22 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)