A3M7Z0 (SERC_ACIBT) 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:	A1S_2617

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

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: 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 – 359	359	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000097201
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)
	A3M7Z0 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 3ED422F4DD91B746	FASTA	359	39,281
	10 20 30 40 50 60 MRAYNFCAGP AALPTAVLEK AQQELLDWQG KGLSIMEMSH RSADYVAVAE KAEADLRKLM 70 80 90 100 110 120 NIPENYKVLF LQGGASLQFS AIPLNLLGKN NKADYIHTGI WSEKALKEAK RYGDINVVEA 130 140 150 160 170 180 GIKVDGKFAI SEQSEWNLSD DAAYVHYADN ETIGGLQFAG VPDVKAPLVC DFSSSILSAP 190 200 210 220 230 240 LDVSKFGLIY AGAQKNIGPA GLTIVIIRDD LLDQAKAEIP SILKYADQAK NGSMVNTPST 250 260 270 280 290 300 YAWYLSGLVF EWLLEQGGVD AIHKVNLEKA QLLYGYIDSS DFYNNPIAIP NRSIMNVPFT 310 320 330 340 350 LADEALEKQF LKEAEANHLL NLAGHRSVGG MRASIYNAVP LEGVQALIRF MDDFAKRNG

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000521 Genomic DNA. Translation: ABO13034.2.
RefSeq	YP_001085636.2. NC_009085.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A3M7Z0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4917897.
GenomeReviews	Gene locus A1S_2617 in contig CP000521_GR.
KEGG	acb:A1S_2617.
NMPDR	fig|400667.4.peg.2720.
PATRIC	20721537. VBIAciBau103176_2664.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HBG289982.
ProtClustDB	PRK05355.
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_ACIBT

Accession

Primary (citable) accession number: A3M7Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 2, 2008
Last modified:	December 14, 2011
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program