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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 3 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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei195Thiamine pyrophosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

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:pdhAbeta
Ordered Locus Names:ZMO1605
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622371 – 462Pyruvate dehydrogenase E1 component subunit betaAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotation1

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

3D structure databases

ProteinModelPortaliO66113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 78Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77

Sequence similaritiesi

Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

HOGENOMiHOG000281450.
KOiK00162.
OMAiRKTHHLV.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIELKMPAL SPTMEEGTLT RWLVKEGDSI KAGEILAEIE TDKAIMEFEA
60 70 80 90 100
VDEGVITKIL IPEGSENVKV GTAIAYLGTD ANDVTLDGAS AETKAEESAP
110 120 130 140 150
VASPAKTEAA AVEEAATPSL GKVINSAPEI PEGTEFFQQT LREALRDAMA
160 170 180 190 200
EEMRRDDRVF VMGEEVAEYQ GAYKVTQGLL QEFGARRVVD TPISEYGFSG
210 220 230 240 250
IGVGAAMEGL RPVIEFMTMN FSMQAIDHII NSAAKTHYMS GGQVRCPIVF
260 270 280 290 300
RGPNGAAPRV GAQHTQNFGP WYAAVPGLVV LAPYDAIDAK GLLKAAIRSD
310 320 330 340 350
DPVVFLECEL LYGKTFDVPK MDDFVLPIGK ARIIREGKDV TIVSYSIGVS
360 370 380 390 400
FALTAAEALA KEGIDAEVID LRTLRPLDKE TILQSLAKTN RIVTVEDGWP
410 420 430 440 450
VCSISSEIAA IAMEEGFDNL DAPVLRVTNA DTPTPYAENL EKKGLVNPEA
460
IIEAVRKVCY RK
Length:462
Mass (Da):49,833
Last modified:February 15, 2005 - v2
Checksum:i00F53CE4A5731F1C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87D → E in CAA73385 (PubMed:9515924).Curated1
Sequence conflicti112V → L in CAA73385 (PubMed:9515924).Curated1
Sequence conflicti232 – 244SAAKT…SGGQV → LRPKRIICPAAKC (Ref. 2) CuratedAdd BLAST13
Sequence conflicti259R → P in AAC70362 (Ref. 2) Curated1
Sequence conflicti262A → E in AAC70362 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12884 Genomic DNA. Translation: CAA73385.1.
AF086791 Genomic DNA. Translation: AAC70362.1.
AE008692 Genomic DNA. Translation: AAV90229.1.
PIRiT33723.
RefSeqiWP_011241359.1. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV90229; AAV90229; ZMO1605.
KEGGizmo:ZMO1605.
PATRICi32568468. VBIZymMob102260_1510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12884 Genomic DNA. Translation: CAA73385.1.
AF086791 Genomic DNA. Translation: AAC70362.1.
AE008692 Genomic DNA. Translation: AAV90229.1.
PIRiT33723.
RefSeqiWP_011241359.1. NC_006526.2.

3D structure databases

ProteinModelPortaliO66113.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV90229; AAV90229; ZMO1605.
KEGGizmo:ZMO1605.
PATRICi32568468. VBIZymMob102260_1510.

Phylogenomic databases

HOGENOMiHOG000281450.
KOiK00162.
OMAiRKTHHLV.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODPB_ZYMMO
AccessioniPrimary (citable) accession number: O66113
Secondary accession number(s): O69012, Q5NM31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.