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A4XA60 (A4XA60_SALTO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. 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:Strop_3373
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP] EMBL ABP55806.1
Taxonomic identifier369723 [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
A4XA60 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: D66CE5A9A14CF2C2

FASTA912101,714
        10         20         30         40         50         60 
MATERKRPVI SAGLPSQLPD IDPDETGEWV ESLDGVVDER GTKRARYVML RLLERARERQ 

        70         80         90        100        110        120 
VGVPSLTTTD YINTIAPERE PWFPGDEHVE RRIRAYIRWN AAVLVHRAQR PDIGVGGHIS 

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

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

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

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

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

       430        440        450        460        470        480 
HQMKKLTLDD LKTFRDRLYL DIPDKALEEN PYLPPYYRPE AKSDEIEYLH ERRRQLGGYL 

       490        500        510        520        530        540 
PSRRPGTKRL TIPGPESFAD VKRGSGKQKV ATTMAFNRLL KDLMKDREFG QRWVPIIPDE 

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

       610        620        630        640        650        660 
SAYATHNEPM IPMYIFYSMF GFQRTADGLW AAADQMARGF LLGATAGRTT LNGEGLQHED 

       670        680        690        700        710        720 
GHSLLIAATN PAVVAYDPAF AFEIAHIVEN GLHRMYGEAQ ENVFYYLTVY NEPIVQPAEP 

       730        740        750        760        770        780 
AEVDVEGILK GIYRYSPAPQ VDGPPAQLLA SGTGLQWALK AQDLLARDWG VAASVWSVTS 

       790        800        810        820        830        840 
WTELRRDAVQ AEEHNLLNPT GEQQVPYVAA KLADADGPKV AVSDWMRAVP DLISRWVPGD 

       850        860        870        880        890        900 
YTSLGTCGFG MSDTRHALRR YFHVDAESIV VATLRQLALR GAVPAGVPAE AAKKYAIDDV 

       910 
GAAPVGETGG DS

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000667 Genomic DNA. Translation: ABP55806.1.
RefSeqYP_001160184.1. NC_009380.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4XA60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5059840.
GenomeReviewsGene locus Strop_3373 in contig CP000667_GR.
KEGGstp:Strop_3373.
PATRIC23445878. VBISalTro43511_3478.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2609.
HOGENOMHBG289271.
OMAFRQEKSH.
PhylomeDBA4XA60.
ProtClustDBPRK09405.

Enzyme and pathway databases

BioCycSTRO369723:STROP_3373-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 nameA4XA60_SALTO
AccessionPrimary (citable) accession number: A4XA60
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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