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Q638W1 (SERC_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:BCE33L2969
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length360 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 – 360360Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150146

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region237 – 2382Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1521Pyridoxal phosphate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site1951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q638W1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: A4E535B79FED4F83

FASTA36040,447
        10         20         30         40         50         60 
MERVYNFSAG PSILPLPVLE KVQKELVNYN GTGMSIMEMS HRSSYFQSII DEASNLLREL 

        70         80         90        100        110        120 
MNIPNEYDVL FLQGGASLQF SMIPLNLMNT YKKAGYVLTG SWSKKALQEA EKVGEVQVIA 

       130        140        150        160        170        180 
SSENEKFTTI PKLDGLLGDE KLDYVHITTN NTIEGTKYVD IPRVDKVPLV ADMSSNILSE 

       190        200        210        220        230        240 
RYDVSKFGLI YAGAQKNLGP AGLTIAIIKR DLIGGADRYC PTMLNYETYS KNNSLYNTPP 

       250        260        270        280        290        300 
SFSIYVTKLV LEWLKEQGGV SAIEEQNKMK SSLLYNFLDE SKLFTSPVDP TYRSLMNIPF 

       310        320        330        340        350        360 
TTPSEELNNE FLQKAKERGL VTLKGHRSVG GMRASIYNAM PVQGVQQLVN YMKEFELENR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000001 Genomic DNA. Translation: AAU17292.1.
RefSeqYP_084556.1. NC_006274.1.

3D structure databases

ProteinModelPortalQ638W1.
SMRQ638W1. Positions 1-356.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ638W1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000043042; EBBACP00000041943; EBBACG00000043033.
GeneID3025081.
GenomeReviewsGene locus BCE33L2969 in contig CP000001_GR.
KEGGbcz:BCZK2969.
PATRIC18889616. VBIBacCer95304_3146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1932.
GeneTreeEBGT00050000002587.
HOGENOMHBG289982.
OMAYEVLFLQ.
PhylomeDBQ638W1.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycBCER288681:BCE33L2969-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_BACCZ
AccessionPrimary (citable) accession number: Q638W1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 60 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

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