Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Pyropia yezoensis (Susabi-nori) (Porphyra yezoensis)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei60Thiamine pyrophosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandPyruvate, 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
OrganismiPyropia yezoensis (Susabi-nori) (Porphyra yezoensis)
Taxonomic identifieri2788 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeBangialesBangiaceaePyropia

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002772541 – 331Pyruvate dehydrogenase E1 component subunit betaAdd BLAST331

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ1XDM1
SMRiQ1XDM1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.920, 1 hit
InterProiView protein in InterPro
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005475 Transketolase-like_Pyr-bd
IPR033248 Transketolase_C
PfamiView protein in Pfam
PF02779 Transket_pyr, 1 hit
PF02780 Transketolase_C, 1 hit
SMARTiView protein in SMART
SM00861 Transket_pyr, 1 hit
SUPFAMiSSF52518 SSF52518, 1 hit
SSF52922 SSF52922, 1 hit

Sequencei

Sequence statusi: Complete.

Q1XDM1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIFMFDAL RAATDEEMAK DPTVCVIGED VGHYGGSYKV TKDLHSKYGD
60 70 80 90 100
LRVLDTPIAE NSFTGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM
110 120 130 140 150
LRYTSGGNFT LPLVIRGPGG VGRQLGAEHS QRLEAYFQAI PGLKIVACST
160 170 180 190 200
PYNAKGLLKS AIRDNNPVVF FEHVLLYNLQ EEIPQEEYFL PLNKVEFVRK
210 220 230 240 250
GKDITILTYS RMRHHVIQAL PALLKEGYDP EVIDLISLKP LDIDSISISV
260 270 280 290 300
KKTHKVLIVE ECMKTAGIGA ELIAQINEYL FDELDAPVVR LSSQDIPTPY
310 320 330
NGSLEQATVI QPSQIVDSVK SIITSVKAII T
Length:331
Mass (Da):36,385
Last modified:May 2, 2006 - v1
Checksum:i8F8C892E9684F733
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006715 Genomic DNA Translation: BAE92390.1
RefSeqiYP_536947.1, NC_007932.1

Genome annotation databases

GeneIDi3978894

Similar proteinsi

Entry informationi

Entry nameiODPB_PYRYE
AccessioniPrimary (citable) accession number: Q1XDM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: May 2, 2006
Last modified: October 25, 2017
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health