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J9YBT2

- J9YBT2_ALTMA

UniProt

J9YBT2 - J9YBT2_ALTMA

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

MASE_14020

Organism
Alteromonas macleodii ATCC 27126
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

Keywords - Ligandi

PyruvateImported

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
ORF Names:MASE_14020Imported
OrganismiAlteromonas macleodii ATCC 27126Imported
Taxonomic identifieri529120 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
ProteomesiUP000006102: 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

Structurei

3D structure databases

ProteinModelPortaliJ9YBT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 3 lipoyl-binding domains.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

KOiK00627.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

J9YBT2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDIQKIIVP DVGGDEVEVI ELCVAVGDNI EADEGVVTVE SDKASMDIPA
60 70 80 90 100
PFEGEIVSLT VSVGDKIKEG DVIGEMKVAN GDSADKGASE ENASDESSKE
110 120 130 140 150
DAPKQEEAPK DESKSEAAPA ASGSSEVIEV AVPDIGSDDE VDVIDVLVSV
160 170 180 190 200
GDTIEKEDGL ITLETDKATM DVPSTHAGTV KEVFISTGDK VKEGTVVIKL
210 220 230 240 250
EVAGSGSSSS ESASSDASSE ASAPAAQESA KQESAPAASS GSETIEVAVP
260 270 280 290 300
DIGEDGEVDV IDVLVSAGDT VEKEDGLITL ETDKATMDVP STHAGTIKEV
310 320 330 340 350
FIKAGDKVKQ GTLVVKLETS GGSSSSAAEK PAEAPKQEET KQDSQQEETQ
360 370 380 390 400
QASQQEASQG RSPVPPAPEA KNTGKAHASP SVRRIAREFG VDLTQVNGSG
410 420 430 440 450
PKNRILKEDV QAYVKAELAK PRTAAASGSA PVGDNVLQIV PVKPVDHSKF
460 470 480 490 500
GEIEEQKLSR IQKISGPFLH RNWATIPHVT QFDEADITEV EEFRKEQNAY
510 520 530 540 550
HAKIKSGLKI TPLVFVMKAV AKALEKYEVF NSSLSDDGES LIIKKFINIG
560 570 580 590 600
IAVETPGGLV VPVIRDVNKK GIEQLSQELI DTSKKAREGK LKAADMQGGT
610 620 630 640 650
FTISSLGGIG GTAFTPIVNA PEVAILGVSK SEMKPKWNGK EFEPRLMVPL
660 670 680
SLSYDHRVID GAVGARFSTE VAANLTDLRR IIL
Length:683
Mass (Da):71,912
Last modified:November 28, 2012 - v1
Checksum:i67B13B76E78A3848
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003841 Genomic DNA. Translation: AFS38308.1.
RefSeqiWP_014950395.1. NC_018632.1.
YP_006748862.1. NC_018632.1.

Genome annotation databases

EnsemblBacteriaiAFS38308; AFS38308; MASE_14020.
GeneIDi13669711.
KEGGiamac:MASE_14020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003841 Genomic DNA. Translation: AFS38308.1 .
RefSeqi WP_014950395.1. NC_018632.1.
YP_006748862.1. NC_018632.1.

3D structure databases

ProteinModelPortali J9YBT2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFS38308 ; AFS38308 ; MASE_14020 .
GeneIDi 13669711.
KEGGi amac:MASE_14020.

Phylogenomic databases

KOi K00627.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
    Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
    ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27126Imported.

Entry informationi

Entry nameiJ9YBT2_ALTMA
AccessioniPrimary (citable) accession number: J9YBT2
Entry historyi
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: November 26, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3