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B0U862

- B0U862_METS4

UniProt

B0U862 - B0U862_METS4

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene
M446_6300
Organism
Methylobacterium sp. (strain 4-46)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.UniRule annotation

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.UniRule annotation
Binds 2 lipoyl cofactors covalently By similarity.UniRule annotation
Binds 3 lipoyl cofactors covalently By similarity.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: InterPro

GO - Biological processi

  1. glycolytic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Enzyme and pathway databases

BioCyciMSP426117:GI2I-6376-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Ordered Locus Names:M446_6300Imported
OrganismiMethylobacterium sp. (strain 4-46)Imported
Taxonomic identifieri426117 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
ProteomesiUP000001185: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi426117.M446_6300.

Structurei

3D structure databases

ProteinModelPortaliB0U862.
SMRiB0U862. Positions 3-81, 139-183, 198-440.

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 1 lipoyl-binding domain.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotations

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiFWHVSEG.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B0U862-1 [UniParc]FASTAAdd to Basket

« Hide

MATEVKVPDI GDFKDVPIIE VHVKEGDTIG PDDPIISLES DKATMEVPAP    50
SGGVVEKLLI KIGDKVSEGH PILLLKGEGD AKGDATSAPR SESESKGNGA 100
APADTAALIA KQEPPESAAP PAPVPAPAAS GAGIPDFSQI HASPAVRRLA 150
RELGVDLNAI KGTGEKGRIT KEDVKGHLTR SAAPAPSGAV FAGGGMGIPE 200
IPAVDFSKFG PTETKPLARI KKISGPHLHR AWLNVPLVTH QDEADITETE 250
AYRKDLDKTA KDKGYRVTLL AFLIKASVSA LRQHPEFNAS LSPDKEALIL 300
KRYYNIGVAV DTPDGLVVPV VKDADRKGIG EISQELGALS KKARDGKLGS 350
GDMQGASFTI SSLGGIGGTA FTPLVNAPEV AILGVVRSRM APVWDGSEFK 400
PRLMLPLSVS YDHRVIDGAL AARFTRHLAH VLEDVRRLVI 440
Length:440
Mass (Da):46,287
Last modified:April 8, 2008 - v1
Checksum:i5ECC6C0985075A9E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000943 Genomic DNA. Translation: ACA20566.1.
RefSeqiWP_012335944.1. NC_010511.1.
YP_001773000.1. NC_010511.1.

Genome annotation databases

EnsemblBacteriaiACA20566; ACA20566; M446_6300.
GeneIDi6135502.
KEGGimet:M446_6300.
PATRICi22593891. VBIMetSp32184_6245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000943 Genomic DNA. Translation: ACA20566.1 .
RefSeqi WP_012335944.1. NC_010511.1.
YP_001773000.1. NC_010511.1.

3D structure databases

ProteinModelPortali B0U862.
SMRi B0U862. Positions 3-81, 139-183, 198-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 426117.M446_6300.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA20566 ; ACA20566 ; M446_6300 .
GeneIDi 6135502.
KEGGi met:M446_6300.
PATRICi 22593891. VBIMetSp32184_6245.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
KOi K00627.
OMAi FWHVSEG.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci MSP426117:GI2I-6376-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 4-46Imported.

Entry informationi

Entry nameiB0U862_METS4
AccessioniPrimary (citable) accession number: B0U862
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: September 3, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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