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G8UF64 (G8UF64_BACCE) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 12. Feed History...

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

Protein namesRecommended name:
Phosphoserine aminotransferase RuleBase RU004505 HAMAP-Rule MF_00160
EC=2.6.1.52 RuleBase RU004505 HAMAP-Rule MF_00160
Alternative name(s):
Phosphohydroxythreonine aminotransferase HAMAP-Rule MF_00160
Gene names
Name:serC HAMAP-Rule MF_00160
ORF Names:bcf_16170 EMBL AEW56356.1
OrganismBacillus cereus F837/76 EMBL AEW56356.1
Taxonomic identifier347495 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › 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. SAAS SAAS020578 HAMAP-Rule MF_00160

Catalytic activity

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. SAAS SAAS020578 HAMAP-Rule MF_00160

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. SAAS SAAS020578 RuleBase RU004505 HAMAP-Rule MF_00160

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. SAAS SAAS020578 HAMAP-Rule MF_00160

Pyridoxal phosphate By similarity. RuleBase RU004504

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. SAAS SAAS020578 RuleBase RU004505 HAMAP-Rule MF_00160

Subunit structure

Homodimer By similarity. SAAS SAAS020578 HAMAP-Rule MF_00160

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00160.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. HAMAP-Rule MF_00160

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region76 – 772Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00160
Region237 – 2382Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00160

Sites

Binding site421L-glutamate By similarity HAMAP-Rule MF_00160
Binding site1021Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1521Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1721Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1951Pyridoxal phosphate By similarity HAMAP-Rule MF_00160

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00160

Sequences

Sequence LengthMass (Da)Tools
G8UF64 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: F29B94B8B41A720B

FASTA36040,418
        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 PKLDGLLGDE KLDYVHITTN NTIEGTKYMD IPHVDKVPLV 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

References

[1]"Complete Genome Sequence of the Highly Hemolytic Strain Bacillus cereus F837/76."
Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P., Sorokin A.
J. Bacteriol. 194:1630-1630(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F837/76 EMBL AEW56356.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003187 Genomic DNA. Translation: AEW56356.1.
RefSeqYP_005119869.1. NC_016779.1.

3D structure databases

ProteinModelPortalG8UF64.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW56356; AEW56356; bcf_16170.
GeneID11680223.
KEGGbcf:bcf_16170.

Phylogenomic databases

KOK00831.

Enzyme and pathway databases

UniPathwayUPA00135; UER00197.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
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 nameG8UF64_BACCE
AccessionPrimary (citable) accession number: G8UF64
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: April 3, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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