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C6S7H7

- C6S7H7_NEIML

UniProt

C6S7H7 - C6S7H7_NEIML

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Neisseria meningitidis (strain alpha14)
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 annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Enzyme and pathway databases

BioCyciNMEN662598:GJMX-1173-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:NMO_1180Imported
OrganismiNeisseria meningitidis (strain alpha14)Imported
Taxonomic identifieri662598 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002054: 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

STRINGi662598.NMO_1180.

Structurei

3D structure databases

ProteinModelPortaliC6S7H7.
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

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.
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.

C6S7H7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA
60 70 80 90 100
DAAGVVKEVK VKVGDKISEG GVILTVETGA AAAEAASAAA EAQPAPAAAP
110 120 130 140 150
VAAGGATVQV AVPDIGGHTD VDVIAVEIKV GDTVAEDDTL ITLETDKATM
160 170 180 190 200
DVPCTAAGVV KAVFLKVGDK VSEGSAIIEV ETVGSAAAAP AQAAQAAAPA
210 220 230 240 250
AAPPPTAAAA PAAAPAPSAP AAAKIDEAAF AKAHAGPSAR KLARELGVDL
260 270 280 290 300
GQVKGTGLKG RIVGDDIKAF VKSVMQGGAA KPAAAGASLG SGLDLLPWPK
310 320 330 340 350
VDFSKFGNVE VKELSRIKKI SGQNLSRNWV VIPHVTVHEE ADMTELEEFR
360 370 380 390 400
KQLNKEWERE GVKLSPLAFI IKASVSALKA FPEFNASLDG DNLVLKNYFN
410 420 430 440 450
IGFAADTPNG LVVPVIKDVD QKGLKQISQE LTELSKKARE GKLKPQEMQG
460 470 480 490 500
ACFTISSLGG IGGTGFTPIV NAPEVAILGV CKSQIKPVWN GKEFAPRLMC
510 520 530
PLSLSFDHRV IDGAAGMRFT VFLAKLLKDF RRITL
Length:535
Mass (Da):55,209
Last modified:September 22, 2009 - v1
Checksum:iF05F7CDA19624106
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889136 Genomic DNA. Translation: CBA06394.1.
RefSeqiYP_003083358.1. NC_013016.1.

Genome annotation databases

EnsemblBacteriaiCBA06394; CBA06394; NMO_1180.
GeneIDi8222195.
KEGGinmi:NMO_1180.
PATRICi20369083. VBINeiMen141067_1500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889136 Genomic DNA. Translation: CBA06394.1 .
RefSeqi YP_003083358.1. NC_013016.1.

3D structure databases

ProteinModelPortali C6S7H7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 662598.NMO_1180.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBA06394 ; CBA06394 ; NMO_1180 .
GeneIDi 8222195.
KEGGi nmi:NMO_1180.
PATRICi 20369083. VBINeiMen141067_1500.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMEN662598:GJMX-1173-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. "Whole-genome comparison of disease and carriage strains provides insights into virulence evolution in Neisseria meningitidis."
    Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T., Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T., Linke B., Vogel U., Frosch M.
    Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: alpha14Imported.

Entry informationi

Entry nameiC6S7H7_NEIML
AccessioniPrimary (citable) accession number: C6S7H7
Entry historyi
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: November 26, 2014
This is version 38 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