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I1I1P6 (I1I1P6_BRADI) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 9. 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 attributes

Sequence length452 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 By similarity. RuleBase RU361137

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. RuleBase RU361137

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. RuleBase RU361137

Binds 2 lipoyl cofactors covalently By similarity. RuleBase RU361137

Binds 3 lipoyl cofactors covalently By similarity. RuleBase RU361137

Subcellular location

Mitochondrion matrix By similarity RuleBase RU361137.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family. RuleBase RU361137

Contains 1 lipoyl-binding domain. RuleBase RU361137

Sequences

Sequence LengthMass (Da)Tools
I1I1P6 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: A123297671E4EBA4

FASTA45248,418
        10         20         30         40         50         60 
MARANPVTLL PASLAGHYKV GLPPHMVIGM PALSPTMNQG NLAKWRKQEG DKIEVGDVIC 

        70         80         90        100        110        120 
EIETDKATLE FESLEEGYLA KILVPEGSKD VQVGEPIFVT VEESEDIKNI PADTSFGGEQ 

       130        140        150        160        170        180 
KEEQSSGSAA QSVQVDAAET SSVTSRISPA AKMLIKEHGL DASLLKASGP RGTLLKGDVL 

       190        200        210        220        230        240 
AALKSGTASS AKEQTAPVAP SPKPTRDTQA QSPITSQKSD TFEDITNTQI RKVIAKRLLE 

       250        260        270        280        290        300 
SKQTTPHLYL SKDVILDPLL AFRNELKEQH GVKVSVNDIV IKAVALALRN VPEANAYWDT 

       310        320        330        340        350        360 
AKQEAQKCDS VDISIAVATE KGLMTPIIRN ADQKTISAIS SEVKQLAKKA RAGKLAPNEF 

       370        380        390        400        410        420 
QGGSFSISNL GMYPVDHFCA IINPPQAGIL AVGRGNKVVE PVMDSDGTEK AAVLTKMSLT 

       430        440        450 
LSADHRIFDG QVGGKFFTEL ASNFSDIRRL LL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequencing and analysis of the model grass Brachypodium distachyon."
International Brachypodium Initiative
Nature 463:763-768(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Bd21 EnsemblPlants BRADI3G17280.2.
[2]EnsemblPlants
Submitted (NOV-2012) to UniProtKB
Cited for: IDENTIFICATION.
Strain: cv. Bd21 EnsemblPlants BRADI3G17280.2.

Cross-references

Sequence databases

RefSeqXP_003571498.1. XM_003571450.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsBRADI3G17280.2; BRADI3G17280.2; BRADI3G17280.
GeneID100839523.
KEGGbdi:100839523.

Phylogenomic databases

KOK00627.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI1I1P6_BRADI
AccessionPrimary (citable) accession number: I1I1P6
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: July 9, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)