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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Pyropia yezoensis (Susabi-nori) (Porphyra yezoensis)
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)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

Q1XDM1:

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)