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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Zygnema circumcarinatum (Green alga)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
Synonyms:odpB
Encoded oniPlastid; Chloroplast
OrganismiZygnema circumcarinatum (Green alga)
Taxonomic identifieri35869 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaZygnemophyceaeZygnematalesZygnemataceaeZygnema

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Pyruvate dehydrogenase E1 component subunit betaPRO_0000280105Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ32RM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Q32RM2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEVLLFEAL RQGLQEEMDR DPRVMVMGED VGHYGGSYKV TKGFAERYGD
60 70 80 90 100
LRLLDTPIAE NSFTGMAIGA AMTGLRPVVE GMNMGFLLLA FNQIANNAGM
110 120 130 140 150
LHYTSGGNFT IPIVIRGPGG VGRQLGAEHS QRLESYFQSV PGLQMVACST
160 170 180 190 200
PYNAKGLIKS AIRSDNPIIL FEHVLLYNLK EDLAEEEYLV CLEKAEVVRP
210 220 230 240 250
GNDITILTYS RMRHNVLQAT KSLVYKGYDP EIIDIVSLKP FDLGTIGASV
260 270 280 290 300
CKTHKVLIVE ECMRTGGIGA TLRAAIMEHF FDYLDAPILC LSSQDVPTPY
310 320
SSPLEELTVI QPNQIIQVVE QLCEN
Length:325
Mass (Da):35,808
Last modified:March 6, 2007 - v2
Checksum:i0FF32E1811E40420
GO

Sequence cautioni

The sequence AAX45823.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY958086 Genomic DNA. Translation: AAX45823.1. Different initiation.
RefSeqiYP_636504.1. NC_008117.1.

Genome annotation databases

GeneIDi4108143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY958086 Genomic DNA. Translation: AAX45823.1. Different initiation.
RefSeqiYP_636504.1. NC_008117.1.

3D structure databases

ProteinModelPortaliQ32RM2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4108143.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete chloroplast DNA sequences of the charophycean green algae Staurastrum and Zygnema reveal that the chloroplast genome underwent extensive changes during the evolution of the Zygnematales."
    Turmel M., Otis C., Lemieux C.
    BMC Biol. 3:22-22(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiODPB_ZYGCR
AccessioniPrimary (citable) accession number: Q32RM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: January 7, 2015
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.