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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.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Note: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • Note: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • Note: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
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.UniRule annotation

Protein-protein interaction databases

STRINGi426117.M446_6300.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

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

        10         20         30         40         50
MATEVKVPDI GDFKDVPIIE VHVKEGDTIG PDDPIISLES DKATMEVPAP
60 70 80 90 100
SGGVVEKLLI KIGDKVSEGH PILLLKGEGD AKGDATSAPR SESESKGNGA
110 120 130 140 150
APADTAALIA KQEPPESAAP PAPVPAPAAS GAGIPDFSQI HASPAVRRLA
160 170 180 190 200
RELGVDLNAI KGTGEKGRIT KEDVKGHLTR SAAPAPSGAV FAGGGMGIPE
210 220 230 240 250
IPAVDFSKFG PTETKPLARI KKISGPHLHR AWLNVPLVTH QDEADITETE
260 270 280 290 300
AYRKDLDKTA KDKGYRVTLL AFLIKASVSA LRQHPEFNAS LSPDKEALIL
310 320 330 340 350
KRYYNIGVAV DTPDGLVVPV VKDADRKGIG EISQELGALS KKARDGKLGS
360 370 380 390 400
GDMQGASFTI SSLGGIGGTA FTPLVNAPEV AILGVVRSRM APVWDGSEFK
410 420 430 440
PRLMLPLSVS YDHRVIDGAL AARFTRHLAH VLEDVRRLVI
Length:440
Mass (Da):46,287
Last modified:April 8, 2008 - v1
Checksum:i5ECC6C0985075A9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3