Q5X5E7 (SERC_LEGPA) 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:	lpp1373

Organism

Legionella pneumophila (strain Paris) [Complete proteome] [HAMAP]

Taxonomic identifier

297246 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	362 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 – 362	362	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150178
Regions
	Region	77 – 78	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	43	1	L-glutamate By similarity
	Binding site	103	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)
	Q5X5E7 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 7D187A7D5D49D425	FASTA	362	40,831
	10 20 30 40 50 60 MNSRVFNFGA GPAMLPEEIL KEAQEEFLNW RNTGMSILEI GHRTPEIINL LSTAEQSLRE 70 80 90 100 110 120 LLNIPKNYHV LFLGGAARAQ FAMIPMNLLQ PGDEAAYFIT GIWSKMAYHE ANLLKQAYYL 130 140 150 160 170 180 SNEEKEGFVS IPDYQKWELK SNTPYVYYTP NETINGVRFP YVPKTGGVPL VADMTSCLLS 190 200 210 220 230 240 EPININQYGL IFAGAQKNIA NAGLTIVIIH EDLLKNQPEP AIPTMLNYKN HAEHRSLYAT 250 260 270 280 290 300 PPVFNCYLAS KMFEWIKTQG GIEGVFQRNC LKAAKLYQYL DSTDFYLTPV SKEARSIMNI 310 320 330 340 350 360 CFSLCYPDLE QKFLDMANKR GLKALKGHRF TGGLRASLYN AMPMAGVDAL IEFMSEFAKE NG

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Paris.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628336 Genomic DNA. Translation: CAH12524.1.
RefSeq	YP_123697.1. NC_006368.1.
3D structure databases
ProteinModelPortal	Q5X5E7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5X5E7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3116490.
GenomeReviews	Gene locus lpp1373 in contig CR628336_GR.
KEGG	lpp:lpp1373.
PATRIC	22323121. VBILegPne27771_1619.
Organism-specific databases
LegioList	lpp1373.
CMR	Search...
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HBG289982.
OMA	YEVLFLQ.
PhylomeDB	Q5X5E7.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	LPNE297246:LPP1373-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_LEGPA

Accession

Primary (citable) accession number: Q5X5E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program