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Q5R0P0

- Q5R0P0_IDILO

UniProt

Q5R0P0 - Q5R0P0_IDILO

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
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

Enzyme and pathway databases

BioCyciILOI283942:GI0U-462-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:aceFImported
Ordered Locus Names:IL0459Imported
OrganismiIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)Imported
Taxonomic identifieri283942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina
ProteomesiUP000001171: 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

STRINGi283942.IL0459.

Structurei

3D structure databases

ProteinModelPortaliQ5R0P0.
SMRiQ5R0P0. Positions 5-82, 351-591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5R0P0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADQIELKVP DVGGEEVEVI EILVSEGDTV EQEDGIVTVE SDKASMDIPA
60 70 80 90 100
SSGGKITELK VKVGDTISEG DVLAMIEASG GADESDESDS EEEAEDKTDD
110 120 130 140 150
KADEEATKDK AEESEDKQEE EKDEDSEPEK KSSGGGSKVI DVEVPDIGDE
160 170 180 190 200
EDVEIIEILV SKGDSVSAED GLITLETDKA TMDVPCPEDG EIEEMLVKVG
210 220 230 240 250
DKVSQGSVIA KLKVSGGADD SEAEEKDSAK EEKSESNKES DKDSGKKSED
260 270 280 290 300
KDQKKDSGSS VKPSSERQPP VPDHPSQRSD RKEGILHASP AVRRVAREFG
310 320 330 340 350
VDLSQVKGSG PKDRILKEDV QEFVKYELSR PKAVAGATGQ GGGGLQVIDP
360 370 380 390 400
PKVDFSKFGE VEEVQLSRIQ RKSGPNLHRN WVTIPHVTQF DEADITELEN
410 420 430 440 450
FRKSENEVAK KKDLGFKITP LVFILKACAK GLREFPTFNS SLSESGESLY
460 470 480 490 500
MKKYVNIGVA VDTPNGLVVP VIRDVDKKGI YELSEELVEI SSKARDGKLK
510 520 530 540 550
ATDMQGGCFS ISSLGGIGGT AFTPIVNAPD VAILGVSRNE MKPKWNGKEF
560 570 580 590
EPRLTLPLSL SYDHRVIDGA EAARFTAYLS GVLGDIRKLV L
Length:591
Mass (Da):63,846
Last modified:January 4, 2005 - v1
Checksum:iE629A0E5DB153606
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV81302.1.
RefSeqiYP_154851.1. NC_006512.1.

Genome annotation databases

EnsemblBacteriaiAAV81302; AAV81302; IL0459.
GeneIDi3173448.
KEGGiilo:IL0459.
PATRICi22138939. VBIIdiLoi21852_0461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017340 Genomic DNA. Translation: AAV81302.1 .
RefSeqi YP_154851.1. NC_006512.1.

3D structure databases

ProteinModelPortali Q5R0P0.
SMRi Q5R0P0. Positions 5-82, 351-591.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 283942.IL0459.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV81302 ; AAV81302 ; IL0459 .
GeneIDi 3173448.
KEGGi ilo:IL0459.
PATRICi 22138939. VBIIdiLoi21852_0461.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ILOI283942:GI0U-462-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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-735 / DSM 15497 / L2-TRImported.

Entry informationi

Entry nameiQ5R0P0_IDILO
AccessioniPrimary (citable) accession number: Q5R0P0
Entry historyi
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 26, 2014
This is version 73 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