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E1VIG6 (E1VIG6_9GAMM) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 16. 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 HAMAP-Rule MF_00160 RuleBase RU004505
EC=2.6.1.52 HAMAP-Rule MF_00160 RuleBase RU004505
Alternative name(s):
Phosphohydroxythreonine aminotransferase HAMAP-Rule MF_00160
Gene names
Name:serC HAMAP-Rule MF_00160
ORF Names:HDN1F_10250 EMBL CBL44608.1
Organismgamma proteobacterium HdN1 EMBL CBL44608.1
Taxonomic identifier83406 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria ›

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-Rule MF_00160 SAAS SAAS020578

Catalytic activity

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

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

Cofactor

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

Pyridoxal phosphate By similarity. RuleBase RU004504

Pathway

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

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. HAMAP-Rule MF_00160 SAAS SAAS020578

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

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
E1VIG6 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: DC9F41AF83DBAA5F

FASTA36039,576
        10         20         30         40         50         60 
MARAFNFCAG PAALPEEVLT QASAEMLDYQ GRGLSVMEMS HRSAEFVAIA EQAEKDLREL 

        70         80         90        100        110        120 
LQIPANYKVL FLSGGAHLQF AMVPLNLLAG KTDADYVNTG QWSKRAISEA QRYCAVNVVA 

       130        140        150        160        170        180 
SDEVNRFTGV PDVSSWRRNP DAAYLHYVAN ETIGGVEFDF VPDAEGVPLV VDMSSNILSR 

       190        200        210        220        230        240 
PIDVNQYGLI YAGAQKNIGP AGLTVAIVRE DLLGNAHPST PTMLDYKTHA DNGSMYNTPP 

       250        260        270        280        290        300 
TYAWYLAGLV FQWIQRQGGL GAIEKLNRAK AEKLYRFIDN SGFYKNPVAV ANRSLMNVPF 

       310        320        330        340        350        360 
TLADASLDKS FLQEAEQRHL LNLKGHRSVG GMRASIYNAV PMAAVDALID FMTDFQKRRG

« Hide

References

[1]"Alkane degradation by a new type of denitrifying bacterium with possible involvement of the electron acceptor in substrate activation."
Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P., Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.
Environ. Microbiol. 0:0-0(2010)
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FP929140 Genomic DNA. Translation: CBL44608.1.
RefSeqYP_003810265.1. NC_014366.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBL44608; CBL44608; HDN1F_10250.
GeneID9702867.
KEGGgpb:HDN1F_10250.
PATRIC42344907. VBIGamPro61291_1115.

Phylogenomic databases

HOGENOMHOG000088965.
KOK00831.

Enzyme and pathway databases

BioCycGPRO83406:GIWA-1026-MONOMER.
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 nameE1VIG6_9GAMM
AccessionPrimary (citable) accession number: E1VIG6
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: April 3, 2013
This is version 16 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