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I0A7L1 (I0A7L1_SALET) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 9. Feed History...

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

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
I0A7L1 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 8A8ED1A74D313507

FASTA36239,855
        10         20         30         40         50         60 
MAQVFNFSSG PAMLPAEVLK LAQQELRDWH GLGTSVMEIS HRGKEFIQVA EEAEQDFRDL 

        70         80         90        100        110        120 
LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG YWAASAIKEA KKYCAPQIID 

       130        140        150        160        170        180 
AKITVDGKRA VKPMREWQLS DNAAYLHYCP NETIDGIAID ETPDFGPEVV VTADFSSTIL 

       190        200        210        220        230        240 
SAPLDVSRYG VIYAGAQKNI GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT 

       250        260        270        280        290        300 
PPTFAWYLSG LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV 

       310        320        330        340        350        360 
PFQLADNALD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL TDFMIDFERR 


HG 

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References

[1]"Complete Genome Sequence of the Strong Mutator Salmonella enterica subsp. enterica Serotype Heidelberg Strain B182."
Le Bars H., Bousarghin L., Bonnaure-Mallet M., Jolivet-Gougeon A., Barloy-Hubler F.
J. Bacteriol. 194:3537-3538(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B182 EMBL AFH44968.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003416 Genomic DNA. Translation: AFH44968.1.
RefSeqYP_006087242.1. NC_017623.1.

3D structure databases

ProteinModelPortalI0A7L1.
SMRI0A7L1. Positions 3-362.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFH44968; AFH44968; SU5_01606.
GeneID12709685.
KEGGshb:SU5_01606.

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 nameI0A7L1_SALET
AccessionPrimary (citable) accession number: I0A7L1
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: April 3, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)