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A8LZ51 (A8LZ51_SALAI) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. 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:Sare_3613
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP] EMBL ABV99411.1
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Salinispora

Protein attributes

Sequence length912 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
A8LZ51 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 6DA589C0BEE372E0

FASTA912102,018
        10         20         30         40         50         60 
MATERKRPVI TAGLPSQLPD IDPEETGEWV ESLDGVIDDR GTKRARYVML RLLERARERQ 

        70         80         90        100        110        120 
VGVPSLTTTD YINTITPERE PWFPGDEHVE RRIRAYIRWN AAMLVHRAQR PEIGVGGHIS 

       130        140        150        160        170        180 
TFASSASLYE VGFNHFFRGK DHPGGGDHIF YQGHASPGMY ARAFLEGRLS EHQLDGFRQE 

       190        200        210        220        230        240 
LSHPGGGLPS YPHPRLMPDF WEFPTVSMGL GGVNAIYQAR FNRYLHHRGI KDTSDQHVWA 

       250        260        270        280        290        300 
FLGDGEMDEP ESLGAIGTAA REELDNLTFV INCNLQRLDG PVRGNGKVMQ ELEAFFRGAG 

       310        320        330        340        350        360 
WNVIKVVWGR EWDPLLARDT DGALVNLMNT TPDGDYQTYK AESGAYIREH FFGRDPRTRK 

       370        380        390        400        410        420 
MVEHLSDDEI WNLKRGGHDY RKLYAAYKAA MEHTGQPTVI LAKTIKGWTL GSHFEGRNAT 

       430        440        450        460        470        480 
HQMKKLTLED LKTFRDRLYL DIPDKALEEN PYLPPYYRPE AKSDELEYLH ERRRQLGGYL 

       490        500        510        520        530        540 
PSRRPGTKRL TIPGPERFAD VKRGSGKQKV ATTMAFVRLL KDLMKDREFG RRWVPIVPDE 

       550        560        570        580        590        600 
ARTFGMDSLF PTQKIYSPHG QRYTSVDREL FLSYKEATGG QILHEGINEV GSVASFTAAG 

       610        620        630        640        650        660 
SSYATHDEPM IPMYIFYSMF GFQRTADGLW AAADQMTRGF LLGATAGRTT LNGEGLQHED 

       670        680        690        700        710        720 
GHSLLIAATN PAVVAYDPAF AYEIAHIVEN GLHRMYGAAQ ENVFYYLTVY NEPMVQPAEP 

       730        740        750        760        770        780 
TDVDVEGVLK GIYRYAPAPQ VDGPKAQLLA SGTGMQWALK AQELLAQDWG VAASVWSVTS 

       790        800        810        820        830        840 
WTELRRDAVD AEEHNLLNPT GEQRVPYVTT KLADADGPKV AVSDWMRAVP DLIARWVPGD 

       850        860        870        880        890        900 
YTSLGTCGFG KSDTRHALRR YFHVDAESIV VATLRQLALR GAVPAGVPAE AAKKYAIDDI 

       910 
GAAPVGETGG DS

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000850 Genomic DNA. Translation: ABV99411.1.
RefSeqYP_001538402.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8LZ51.
SMRA8LZ51. Positions 69-904.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8LZ51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5706639.
GenomeReviewsGene locus Sare_3613 in contig CP000850_GR.
KEGGsaq:Sare_3613.
PATRIC23435763. VBISalAre38676_3641.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289271.
OMAFRQEKSH.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycSARE391037:SARE_3613-MONOMER.

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. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA8LZ51_SALAI
AccessionPrimary (citable) accession number: A8LZ51
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: December 14, 2011
This is version 24 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