P57397 (SERC_BUCAI) 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:	BU312

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	361 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 Reference 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 – 361	361	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150158
Regions
	Region	76 – 77	2	Pyridoxal phosphate binding By similarity
	Region	238 – 239	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	102	1	Pyridoxal phosphate By similarity
	Binding site	153	1	Pyridoxal phosphate By similarity
	Binding site	173	1	Pyridoxal phosphate By similarity
	Binding site	196	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57397 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 309BFB2C6D9A05D8	FASTA	361	41,310
	10 20 30 40 50 60 MNLIYNFSAG PAMIPRDVLN QAKKELHNWK NLGSSIMEIS HRSEEFIQMA LEAEKDLRDL 70 80 90 100 110 120 LKIPDSFKVL FCQGGARGQF SAIPMNLLNN LQTADYINSG YWSNSAFMEA KKYCTPRSIF 130 140 150 160 170 180 IRETNGVKES LLPMHKWNIN ENSAYIHYCP NETIDGLSIY EEPVFENKIV VGDFSSFILS 190 200 210 220 230 240 RSINIKNYDL IYAGAQKNIG PAGITIIIIR KNIIGYSSKM TPSILDYKKI SDHHSMFNTP 250 260 270 280 290 300 PTFAWYLSGL VFKWLKKQGG LKAIEKLNKK KSDLLYKKID NSDFYINKIN SKHRSQMNVV 310 320 330 340 350 360 FHLVNPKLNY IFLKEASKTG LNYLRGHSIV GGMRASLYNA MPLEGVESLV KFMSYFEKRY G

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB13020.1.
RefSeq	NP_240134.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57397.
SMR	P57397. Positions 4-361.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002838; EBBUCP00000002614; EBBUCG00000002838.
GeneID	1110011.
GenomeReviews	Gene locus BU312 in contig BA000003_GR.
KEGG	buc:BU312.
PATRIC	21244152. VBIBucAph127364_0324.
Phylogenomic databases
GeneTree	EBGT00050000007909.
HOGENOM	HBG289982.
OMA	VPENYKV.
PhylomeDB	P57397.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	BSP107806:BU312-MONOMER.
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_BUCAI

Accession

Primary (citable) accession number: P57397

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program