P59492 (SERC_BUCBP) 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:	bbp_289

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	373 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 – 373	373	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150160
Regions
	Region	81 – 82	2	Pyridoxal phosphate binding By similarity
	Region	250 – 251	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	47	1	L-glutamate By similarity
	Binding site	113	1	Pyridoxal phosphate By similarity
	Binding site	164	1	Pyridoxal phosphate By similarity
	Binding site	185	1	Pyridoxal phosphate By similarity
	Binding site	208	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	209	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59492 [UniParc]. Last modified April 4, 2003. Version 1. Checksum: 28452E053DF7DFC5	FASTA	373	43,000
	10 20 30 40 50 60 MIMNDTTKVY NFSAGPAMIP REVLCQVKRE LYNWKNLKKS IMEISHRSQE FISVVQEIKH 70 80 90 100 110 120 NLRKLLHIPN SYKIVFCHGG ARGQFSAIPM NFSKNANHSS HNNVVDYINS GYWSYSAALE 130 140 150 160 170 180 AKKYCYTNIL NVCKTNNKKQ YILPMNTWEI NDNSLYLHYC PNETIDGIAI HEEPKFNDKK 190 200 210 220 230 240 IVIGDFSSTI LSKRINLERY SFIYASSQKN IGPSGITLII MHESLLQNIN SYVPSILNYK 250 260 270 280 290 300 ILVNSNSMFN TPNTFSLYLS GLILKWIKKI GGIKEIEKRN IIKSNMLYNM IDSTDFYIND 310 320 330 340 350 360 VVSNNRSRMN VPFTIINTKL HEIFVKEAYK YGLHALKGHN LKGGIRASIY NAMPIKGVLK 370 LINFMKIFEK KYG

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO27014.1.
RefSeq	NP_777909.1. NC_004545.1.
3D structure databases
ProteinModelPortal	P59492.
SMR	P59492. Positions 8-373.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002656; EBBUCP00000002480; EBBUCG00000002656.
GeneID	1058665.
GenomeReviews	Gene locus bbp_289 in contig AE016826_GR.
KEGG	bab:bbp289.
PATRIC	21245365. VBIBucAph80364_0285.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007909.
HOGENOM	HBG289982.
OMA	YEVLFLQ.
PhylomeDB	P59492.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_289-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BUCBP

Accession

Primary (citable) accession number: P59492

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2003
Last sequence update:	April 4, 2003
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program