Reviewed, UniProtKB/Swiss-Prot Q6F961 (SERC_ACIAD)

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:	ACIAD2647

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	359 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 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. 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
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 – 359	359	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150142
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	236 – 237	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	101	1	Pyridoxal phosphate By similarity
	Binding site	152	1	Pyridoxal phosphate By similarity
	Binding site	171	1	Pyridoxal phosphate By similarity
	Binding site	194	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	195	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6F961-1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 91B7C48816B85F89	FASTA	359	39,329
	10 20 30 40 50 60 MRAYNFCAGP AALPTAVLEK AQQELLDWQG KGLSIMEMSH RSKDYVAVAE KAEADLRKLM 70 80 90 100 110 120 NIPENYQVLF LQGGASLQFS AIPMNLLGKN SKADYIHTGI WSEKALKEAQ RYGDINVIEA 130 140 150 160 170 180 GTSIDGKLAI KNQSEWNLSQ DAAYVHYAEN ETIGGIQFAD IPDVNVPLVS DLSSSILSAP 190 200 210 220 230 240 LDVSKFGLIY AGAQKNIGPA GLTIVIVRDD LLDQSRSDIP SILKYSAQAK NGSMVNTPAT 250 260 270 280 290 300 YAWYLSGLVF EWLLEQGGVD AIHQVNLEKA KLLYGYIDSS DFYNNPIAVP NRSIMNVPFT 310 320 330 340 350 LADEALEKLF LQEAEENHLL NLAGHRSVGG MRASIYNAVP LEGVQALVNF MDTFVQKHG

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG69404.1. Different initiation.
RefSeq	YP_047226.2.
3D structure databases
SMR	Q6F961. Positions 2-359.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6F961.
Genome annotation databases
GeneID	2879293.
GenomeReviews	Gene locus ACIAD2647 in contig CR543861_GR.
KEGG	aci:ACIAD2647.
NMPDR	fig|62977.3.peg.2419.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HBG289982.
OMA	TFAWYLA.
PhylomeDB	Q6F961.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD2647-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR003248. Pser_amintransf. 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.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01364. serC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_ACIAD

Accession

Primary (citable) accession number: Q6F961

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	August 16, 2005
Last modified:	February 9, 2010
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)