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G7RAU0 (G7RAU0_ECOC2) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 10. 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 EMBL AER83542.1
Ordered Locus Names:i02_0957 EMBL AER83542.1
OrganismEscherichia coli (strain 'clone D i2') [Complete proteome] [HAMAP]
Taxonomic identifier885276 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length362 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. RuleBase RU004505 SAAS SAAS020578 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

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. 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
Region239 – 2402Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00160

Sites

Binding site91L-glutamate By similarity HAMAP-Rule MF_00160
Binding site421L-glutamate By similarity HAMAP-Rule MF_00160
Binding site1021Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1531Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1741Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1971Pyridoxal phosphate By similarity HAMAP-Rule MF_00160

Amino acid modifications

Modified residue1981N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00160

Sequences

Sequence LengthMass (Da)Tools
G7RAU0 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: CAE21F85AB0B9F14

FASTA36239,771
        10         20         30         40         50         60 
MAQIFNFSSG PAMLPAEVLK QAQQELRDWN GLGTSVMEVS HRGKEFIQVA EEAEKDFRDL 

        70         80         90        100        110        120 
LNVPSNYKVL FCHGGGRGQF AAVPLNILGD KTTADYVDAG YWAASAIKEA KKYCTPNVFD 

       130        140        150        160        170        180 
AKVTVDGLRA VKPMSEWQLS DNAAYMHYCP NETIDGIAID ETPDFGKDVV VAADFSSTIL 

       190        200        210        220        230        240 
SRPIDVSRYG VIYAGAQKNI GPAGLTIVIV REDLLGKANI ACPSILDYSI LNDNDSMFNT 

       250        260        270        280        290        300 
PPTFAWYLSG LVFKWLKANG GVAAMDKINQ QKAELLYGVI DNSDFYRNDV AKANRSRMNV 

       310        320        330        340        350        360 
PFQLADSALD KLFLEESFAA GLHALKGHRV VGGMRASIYN AMPLEGVKAL TDFMVEFERR 


HG

« Hide

References

[1]"Rates of mutation and host transmission for an Escherichia coli clone over 3 years."
Reeves P.R., Liu B., Zhou Z., Li D., Guo D., Ren Y., Clabots C., Lan R., Johnson J.R., Wang L.
PLoS ONE 6:E26907-E26907(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 'clone D i2'.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002211 Genomic DNA. Translation: AER83542.1.
RefSeqYP_006148166.1. NC_017651.1.

3D structure databases

ProteinModelPortalG7RAU0.
SMRG7RAU0. Positions 3-362.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAER83542; AER83542; i02_0957.
GeneID12668726.
KEGGeld:i02_0957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00831.

Enzyme and pathway databases

UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

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 nameG7RAU0_ECOC2
AccessionPrimary (citable) accession number: G7RAU0
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 3, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info