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A1S2I0 (A1S2I0_SHEAM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 46. 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:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156
Gene names
Ordered Locus Names:Sama_0375
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP] EMBL ABL98586.1
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella ›

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity. PIRNR PIRNR000156

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156

Cofactor

Thiamine pyrophosphate By similarity. PIRNR PIRNR000156

Sequences

Sequence LengthMass (Da)Tools
A1S2I0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 9A3BD0C7AA3BCBB4

FASTA898100,265
        10         20         30         40         50         60 
MSEPMQMLQD LDPIETQEWL AALESVVREE GVERAQFLLE QVLEQARLDG VDMPTGITTN 

        70         80         90        100        110        120 
YVNTIPLTQE PAYPGDITIE RRIRSIIRWN AIMIVLRASK KDLELGGHMA SFQSAAAFYE 

       130        140        150        160        170        180 
VCFNHFFRAP NHKDGGDLVY YQGHIAPGIY SRAFLEGRLT EEQLDNFRQE VDGKGISSYP 

       190        200        210        220        230        240 
HPKLMPEFWQ FPTVSMGLGP ISSIYQARFL KYLNGRGLKD TTEQRVYAFL GDGEMDEPES 

       250        260        270        280        290        300 
RGAISFAARE KLDNLCFLIN CNLQRLDGPV MGNGKIIQEL EGLFKGAGWN VIKVVWGSGW 

       310        320        330        340        350        360 
DKLLAKDTTG KLLQLMNETV DGDYQTFKAK DGAYVREHFF GKYPETAALV ADMTDEEIFA 

       370        380        390        400        410        420 
LKRGGHEPSK LYAAFKAAQE TKGRPTVILA KTVKGYGMGD AAEGKNIAHQ VKKMDMSHVA 

       430        440        450        460        470        480 
KLRDRLGVTD LVSDEDLVNL PYIKLEEGSV EHTYLHARRE ALHGYTPKRL PNFTGEFVAP 

       490        500        510        520        530        540 
ELSEFKPLLE EQKRDISTTM GFVRTLNILL KDKNIGKNIV PIIADEARTF GMEGLFRQIG 

       550        560        570        580        590        600 
IYNPYGQNYI PEDRDIVSYY KEDTSGQVLQ EGINELGAMS SWVAAATSYS TNNLPMIPFY 

       610        620        630        640        650        660 
IYYSMFGFQR VGDMAWMAGD QQARGFLLGA TAGRTTLNGE GLQHEDGHSH ILAGTVPNCI 

       670        680        690        700        710        720 
SYDPTFAYET AVIIQDGIRR MYGEQENVFY YLTLMNENYA MPAMPEGAEE GIRKGIYKLE 

       730        740        750        760        770        780 
SHTGGKGSAY SPAKPSKVQL MSSGTIMNEV RKAAVILAEE YGIGSDVFSV TSFNELARNG 

       790        800        810        820        830        840 
QDCERFNMLH PEADARVPYI TSVLGSEPAI AATDYMKNYA EQVRAFMPSV SYKVLGTDGF 

       850        860        870        880        890 
GRSDSRANLR RHFEVNAGYV VVAALNELAK RGDIEKSVVV AAIKKFDIDT EKMNPLYA

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000507 Genomic DNA. Translation: ABL98586.1.
RefSeqYP_926256.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S2I0.
SMRA1S2I0. Positions 59-898.
ModBaseSearch...

Protein-protein interaction databases

STRING326297.Sama_0375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL98586; ABL98586; Sama_0375.
GeneID4602631.
KEGGsaz:Sama_0375.
PATRIC23449303. VBISheAma74963_0386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
HOGENOMHOG000115215.
KOK00163.
OMAAHNTKKV.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycSAMA326297:GH0T-505-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA1S2I0_SHEAM
AccessionPrimary (citable) accession number: A1S2I0
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info