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Q6HGI0 (SERC_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BT9727_3023
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [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_0000150151

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
Q6HGI0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 7463052C1486E016

FASTA36040,366
        10         20         30         40         50         60 
MERVYNFSAG PSILPLPVLE KVQKELVNYN GTGMSIMEMS HRSSYFQSII DEAGSLLREL 

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

       130        140        150        160        170        180 
SSENEKFTTI PKLDGLLGNE KLDYVHITTN NTIEGTKYVD IPHVDKVPLV ADMSSNILSE 

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

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

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

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017355 Genomic DNA. Translation: AAT62315.1.
RefSeqYP_037346.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HGI0.
SMRQ6HGI0. Positions 1-356.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000076162; EBBACP00000074248; EBBACG00000076153.
GeneID2855750.
GenomeReviewsGene locus BT9727_3023 in contig AE017355_GR.
KEGGbtk:BT9727_3023.
NMPDRfig|281309.1.peg.2986.
PATRIC18986984. VBIBacThu119411_3218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002587.
HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_3023-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_BACHK
AccessionPrimary (citable) accession number: Q6HGI0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 59 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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