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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Cyanidium caldarium (Red 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)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
OrganismiCyanidium caldarium (Red alga)
Taxonomic identifieri2771 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeCyanidium

Subcellular locationi

Q9TLS3:

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002801071 – 327Pyruvate dehydrogenase E1 component subunit betaAdd BLAST327

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9TLS3.
SMRiQ9TLS3.
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.

Q9TLS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMMFLYEAL RAAIDEEMGK DSNVFIVGED VGHYGGSYKV TKDLHVKYGD
60 70 80 90 100
LRVLDAPIAE NSFTGMAIGA AMTGLRPIVE GMNMGFMLLA FNQISNNLSM
110 120 130 140 150
LQYTSGGNFN IPVVIRGPGG IGKQLAAEHS QRLESCFQSI PGLQIVACST
160 170 180 190 200
AYNAKGLLKS AIIEKKPILF LEHVLLYNLK GFVPDEEYYL PLDKAEVVRS
210 220 230 240 250
GSDVTIVTYS RMRYHVLAAV EKLVLNGQDP EIIDLISLKP LDLHTISKSI
260 270 280 290 300
KKTHKIVIVE ECAQTGGIAA ELISLINTYL YDELDSPAVR LSSKDVPIPY
310 320
NGNLEKSTLI QPDQIVDVVT NLLQYKT
Length:327
Mass (Da):35,946
Last modified:May 1, 2000 - v1
Checksum:i0697A6E73817EFF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022186 Genomic DNA. Translation: AAF12898.1.
RefSeqiNP_045196.1. NC_001840.1.

Genome annotation databases

GeneIDi800229.

Similar proteinsi

Entry informationi

Entry nameiODPB_CYACA
AccessioniPrimary (citable) accession number: Q9TLS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 1, 2000
Last modified: October 25, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)