Reviewed, UniProtKB/Swiss-Prot A1TSA3 (SERC_ACIAC)

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:	Aave_3281

Organism

Acidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]

Taxonomic identifier

397945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	369 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 – 369	369	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000076903
Regions
	Region	241 – 242	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	101	1	Pyridoxal phosphate By similarity
	Binding site	152	1	Pyridoxal phosphate By similarity
	Binding site	176	1	Pyridoxal phosphate By similarity
	Binding site	199	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	200	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1TSA3-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 9B961C6CFB1B871F	FASTA	369	40,521
	10 20 30 40 50 60 MNRPYNFSAG PAAIPAEVLQ QAASEMLDWH GSGMGVMEMS HRGKEFISIY EQAEADLREL 70 80 90 100 110 120 LAVPQDFRIL FMQGGGLAEN AIVPLNLSRA ATVDMVVTGS WSQKSLKEAR KYASEVHVAA 130 140 150 160 170 180 SAEDSGFTTL PDPASWQLSR GASYLHLCSN ETIHGIEFHE LPDLRALGSD APLVIDFSSH 190 200 210 220 230 240 VASRPVDWSR VGLAFGGAQK NLGPAGLTLV VVREDLLGHA LPACPSAFDY KVVAENQSMF 250 260 270 280 290 300 NTPPTWGIYI AGLTFQWLKR QREGDLSGIA AMEQRNIAKA RLLYNFIDQS QFYVNKVSPN 310 320 330 340 350 360 ARSRMNIPFF LRDETRNEAF LAGARERGLL QLKGHKSVGG MRASLYNAMP LAGVEALVAY MQEFEQRSA

References

[1]

"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000512 Genomic DNA. Translation: ABM33841.1.
RefSeq	YP_971615.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1TSA3.
Genome annotation databases
GeneID	4667688.
GenomeReviews	Gene locus Aave_3281 in contig CP000512_GR.
KEGG	aav:Aave_3281.
NMPDR	fig|397945.5.peg.2805.
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. 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.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_ACIAC

Accession

Primary (citable) accession number: A1TSA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 26 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)