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Q89AQ9

- ODP2_BUCBP

UniProt

Q89AQ9 - ODP2_BUCBP

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Status
Reviewed - 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

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

Cofactori

Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei383 – 3831Sequence Analysis

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

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciBAPH224915:GJ9D-190-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene namesi
Name:aceF
Ordered Locus Names:bbp_190
OrganismiBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic identifieri224915 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000601: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351N6-lipoyllysineBy similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224915.bbp190.

Structurei

3D structure databases

ProteinModelPortaliQ89AQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6868Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
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.
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.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q89AQ9 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPDIGTDLVE VIEILVKIGD QVKKDDSLIT VEGQKASIEI PASHTGTIKN
60 70 80 90 100
IIVHIGEKIT TGSLIAILNG IDDNVKSKND SSSYSFKNSK NTSTNSNLGN
110 120 130 140 150
VNNNINNRTI LVHATPTVRR LARKFDIKLE NITGTGRKGR ILKEDVISYK
160 170 180 190 200
NISLFNDIKK SLKKTNVNYY KDNVTCDDFK SIELTRTQIR SSKNLLKSWL
210 220 230 240 250
TIPHVTQFDE SDITELENFR QKYNSDLKDK SKKLTILIFV IKAVSKALEM
260 270 280 290 300
FPKFNGRLIN KDNRIAIVLN EHINIGIVVD TDDGLLVPVI NRVNKKNISS
310 320 330 340 350
ISNDLRIISE RARSRKLNFS DIKEYGSFTI SNLGGIGGTN FTPIIKYPEL
360 370 380 390 400
AILGISRALI KPYWNSHAFI PKLMLPLSLS YDHRAIDGVA AVRFITFVKK
410
MLTDIRFLMI
Length:410
Mass (Da):46,119
Last modified:June 16, 2003 - v1
Checksum:i69EF982E6C212730
GO

Sequence cautioni

The sequence AAO26922.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26922.1. Different initiation.
RefSeqiNP_777817.1. NC_004545.1.

Genome annotation databases

EnsemblBacteriaiAAO26922; AAO26922; bbp_190.
GeneIDi1058122.
KEGGibab:bbp190.
PATRICi21245155. VBIBucAph80364_0184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016826 Genomic DNA. Translation: AAO26922.1 . Different initiation.
RefSeqi NP_777817.1. NC_004545.1.

3D structure databases

ProteinModelPortali Q89AQ9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224915.bbp190.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO26922 ; AAO26922 ; bbp_190 .
GeneIDi 1058122.
KEGGi bab:bbp190.
PATRICi 21245155. VBIBucAph80364_0184.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BAPH224915:GJ9D-190-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.
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.
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: Bp.

Entry informationi

Entry nameiODP2_BUCBP
AccessioniPrimary (citable) accession number: Q89AQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: October 1, 2014
This is version 79 of the entry and version 1 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

External Data

Dasty 3