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Q031D5 (SERC_LACLS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase

EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Gene names
Name:serC
Ordered Locus Names:LACR_0619
OrganismLactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]
Taxonomic identifier272622 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceInferred 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 processAmino-acid biosynthesis
Serine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionO-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000058214

Regions

Region74 – 752Pyridoxal phosphate binding By similarity
Region241 – 2422Pyridoxal phosphate binding By similarity

Sites

Binding site401L-glutamate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1551Pyridoxal phosphate By similarity
Binding site1771Pyridoxal phosphate By similarity
Binding site2001Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q031D5 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 143E61E7D3B20585

FASTA36540,816
        10         20         30         40         50         60 
MIYNFGAGPS VLPKEVLKKV QEELLDFEKS GMSVMEISHR SKSFQEVIDE AQSNLRDLMS 

        70         80         90        100        110        120 
IPQNYKILFL QGGASTQFSM IPMNLALGKK AYYAISGAFG KKAYDEAVKL SQTLDFEAIS 

       130        140        150        160        170        180 
LGSTQSEHYN HLLKIDKSKV 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 NRQKARMLYD LIDQSDFYQS PVLNEAERSI 

       310        320        330        340        350        360 
CNVVFTSPSK ELDALFVQKA EEKGFKSIKG HRSVGGMRAS IYNAFPIEGV LELVKFMKEF 


EEENK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000425 Genomic DNA. Translation: ABJ72187.1.
RefSeqYP_808609.1. NC_008527.1.

3D structure databases

ProteinModelPortalQ031D5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ031D5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4434091.
GenomeReviewsGene locus LACR_0619 in contig CP000425_GR.
KEGGllc:LACR_0619.
PATRIC22288034. VBILacLac38071_0773.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycLLAC272622:LACR_0619-MONOMER.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. 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]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00831.
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. SerC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_LACLS
AccessionPrimary (citable) accession number: Q031D5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families