Reviewed, UniProtKB/Swiss-Prot A6L5A6 (SERC_BACV8)

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:	BVU_3241

Organism

Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]

Taxonomic identifier

435590 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	356 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 – 356	356	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058200
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	231 – 232	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	99	1	Pyridoxal phosphate By similarity
	Binding site	147	1	Pyridoxal phosphate By similarity
	Binding site	166	1	Pyridoxal phosphate By similarity
	Binding site	189	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	190	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6L5A6-1 [UniParc]. Last modified July 24, 2007. Version 1. Checksum: 402FE1376E764C6E	FASTA	356	39,555
	10 20 30 40 50 60 MKKHNFNAGP SILPREVIEK TAQAVLDFNG SGLSIMEISH RAKDFQPVVD EAVALFKELL 70 80 90 100 110 120 NIPEGYSVLF LGGGASLEFC MIPFNFLEKK AAYLNTGVWA KKAMKEAKAF GEVVEVASSA 130 140 150 160 170 180 EATYTYIPKD YTVPADADYF HVTTNNTIYG TELHEDLDSP VPMIADMSSD IFSRPIDVSK 190 200 210 220 230 240 YICIYGGAQK NLAPAGVTFV IVKNDAVGKV SRYIPTMLNY QTHIDGGSMF NTPPVLPIYA 250 260 270 280 290 300 ALQTLRWIKA NGGVAEMQKR AKEKADMLYA EIDRNKMFRG TVTDKADRSY MNICFVMNDE 310 320 330 340 350 YKDLEADFLK FATEKGMVGI KGHRSVGGFR ASCYNAMPKE SVQALIDCMQ EFEKLH

References

[1]

"Evolution of symbiotic bacteria in the distal human intestine." Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I. PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000139 Genomic DNA. Translation: ABR40870.1.
RefSeq	YP_001300492.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A6L5A6.
Genome annotation databases
GeneID	5304202.
GenomeReviews	Gene locus BVU_3241 in contig CP000139_GR.
KEGG	bvu:BVU_3241.
NMPDR	fig|435590.6.peg.3021.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SMYNTPP.
Family and domain databases
HAMAP	MF_00160. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR003248. Pser_amintransf. [Graphical view]
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
ProDom	PD001544. Pser_amintransf. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01364. serC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BACV8

Accession

Primary (citable) accession number: A6L5A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 24, 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)