A2RIS2 (SERC_LACLM) 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:	llmg_0565

Organism

Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]

Taxonomic identifier

416870 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	365 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
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 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
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 – 365	365	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058213
Regions
	Region	74 – 75	2	Pyridoxal phosphate binding By similarity
	Region	241 – 242	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	40	1	L-glutamate By similarity
	Binding site	99	1	Pyridoxal phosphate By similarity
	Binding site	155	1	Pyridoxal phosphate By similarity
	Binding site	177	1	Pyridoxal phosphate By similarity
	Binding site	200	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	201	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2RIS2 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 3EC97712AB2A1FA5	FASTA	365	40,849
	10 20 30 40 50 60 MIYNFGAGPS VLPKEVLKKV QEELLDFEKS GMSVMEISHR SKSFQEVIDE AQNNLRDLMS 70 80 90 100 110 120 IPQNYKILFL QGGASTQFSM IPMNLALGKK AYYAISGAFG KKAYDEAVKL SQTLDFEAIS 130 140 150 160 170 180 LGSTQSEYYN HLLKIDTSKV DEKMAAYLHI TTNNTIEGTT IFPENLPEVN SVPLIADMSS 190 200 210 220 230 240 NILAVDYDVS KFGLIYAGAQ KNLGIAGLTI VIIREDLLNQ KESLSSMMDY RILAQNGSMY 250 260 270 280 290 300 NTPPTFAIYL AGLVFKWVKE QGGVKKLEAI NHQKARMLYD LIDQSDFYQS PVLNKVERSI 310 320 330 340 350 360 CNVVFTSPSK ELDALFVQKA EEKGFKSIKG HRSVGGMRAS IYNAFPIEGV LELVKFMKKF EEENK

References

[1]

"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MG1363.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM406671 Genomic DNA. Translation: CAL97167.1.
RefSeq	YP_001031913.1. NC_009004.1.
3D structure databases
ProteinModelPortal	A2RIS2.
ModBase	Search...
Protein-protein interaction databases
STRING	A2RIS2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4797974.
GenomeReviews	Gene locus llmg_0565 in contig AM406671_GR.
KEGG	llm:llmg_0565.
PATRIC	22282217. VBILacLac4574_0576.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HBG289982.
OMA	VPENYKV.
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_LACLM

Accession

Primary (citable) accession number: A2RIS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 6, 2007
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program