Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5CRG4 (A5CRG4_CLAM3) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156
Gene names
Name:aceE EMBL CAN01673.1
Ordered Locus Names:CMM_1621
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP] EMBL CAN01673.1
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Clavibacter

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) 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
A5CRG4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: D9DBFB9FEF102D99

FASTA908100,977
        10         20         30         40         50         60 
MTVNDQDPYS VNHTDQDPEE TAEWNESLDG LVETQGRGRA RDVMLSLLKR SKELHLGVPM 

        70         80         90        100        110        120 
VPTTDYINTI APENEPDFPG DEDLERRYRA WIRWNAAVTV HRAQRPGIAV GGHIATYASS 

       130        140        150        160        170        180 
AALYEVGYNH FFRGQDHPGG GDQVFVQGHA SPGTYARAFL EGRLSEHQLD GFRQEKSHAG 

       190        200        210        220        230        240 
GGLSSYPHPR LMPEFWQFPT VSMGLGPINA IYQAQANKYL TNRGIKDASD QQVWAFLGDG 

       250        260        270        280        290        300 
EMDEVESRGQ LQVAANEKLD NLNFVINCNL QRLDGPVRGN GKIIQELESF FRGAGWNVIK 

       310        320        330        340        350        360 
VVWGREWDDL LARDTEGALL DLMNRTPDGD YQTYKAESGA YIRENFFGRD ERTAKLVEGY 

       370        380        390        400        410        420 
TDDQIWNLKR GGHDYRKVYA AFKAASEHTG QPTVILAKTV KGYGLGPSFE GRNATHQMKK 

       430        440        450        460        470        480 
LTLDNLKQFR DEMRVPITDA QLEADPYLPP YYHPGQDDEA IQYMQERRRA LGGYSPERRT 

       490        500        510        520        530        540 
QHTAITLPDD SAYRISKKGS GTQEIATTMA FVRLLKDLIR SKDFGNRVVP IIPDEARTFG 

       550        560        570        580        590        600 
IDAFFPTAKI YNPNGQHYTS VDRELLLSYK ESPQGQIVHV GINEAGALAA FTNLGTTYST 

       610        620        630        640        650        660 
QGEPLIPIYV FYSMFGFQRT GDAIWAAGDQ MARGFLIGAT AGRTTLTGEG LQHADGHSLV 

       670        680        690        700        710        720 
LSQTNPAIVS YDPAYAYEIG HIVRSGLERM YGGEHEDPNV MYYLTVYNEP IIHPSEPEGV 

       730        740        750        760        770        780 
DVDGIVRGVY KLKDGWIDGP KAQLMASGVA VPWALEAQQL LADDWGVSAD VWSVTSWGEL 

       790        800        810        820        830        840 
RRDGLAAEEH NMLHPHSETR VPYLEEKLRH AEGPFVAVTD FSHAVPDQIR QFVPGDYSTL 

       850        860        870        880        890        900 
GADGFGFSDT RPAARRFFAI DGPSMVVKTL QRLAKQGKVD QDAPKWAIDK YRLLDVNAGT 


TGSAGGEA

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM711867 Genomic DNA. Translation: CAN01673.1.
RefSeqYP_001222364.1. NC_009480.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5CRG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5173148.
GenomeReviewsGene locus CMM_1621 in contig AM711867_GR.
KEGGcmi:CMM_1621.
PATRIC21454047. VBIClaMic82482_1740.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
HOGENOMHBG289271.
OMAFRQEKSH.
ProtClustDBPRK09405.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK00163.
PANTHERPTHR11624:SF37. PTHR11624:SF37. 1 hit.
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 nameA5CRG4_CLAM3
AccessionPrimary (citable) accession number: A5CRG4
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 32 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