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C6S7H7

- C6S7H7_NEIML

UniProt

C6S7H7 - C6S7H7_NEIML

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Protein
Acetyltransferase component of pyruvate dehydrogenase complex
Gene
aceF, NMO_1180
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.UniRule annotation
Binds 2 lipoyl cofactors covalently By similarity.UniRule annotation
Binds 3 lipoyl cofactors covalently By similarity.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. glycolytic process Source: InterPro
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 By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi662598.NMO_1180.

Structurei

3D structure databases

ProteinModelPortaliC6S7H7.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotationSAAS annotations

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

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MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA    50
DAAGVVKEVK VKVGDKISEG GVILTVETGA AAAEAASAAA EAQPAPAAAP 100
VAAGGATVQV AVPDIGGHTD VDVIAVEIKV GDTVAEDDTL ITLETDKATM 150
DVPCTAAGVV KAVFLKVGDK VSEGSAIIEV ETVGSAAAAP AQAAQAAAPA 200
AAPPPTAAAA PAAAPAPSAP AAAKIDEAAF AKAHAGPSAR KLARELGVDL 250
GQVKGTGLKG RIVGDDIKAF VKSVMQGGAA KPAAAGASLG SGLDLLPWPK 300
VDFSKFGNVE VKELSRIKKI SGQNLSRNWV VIPHVTVHEE ADMTELEEFR 350
KQLNKEWERE GVKLSPLAFI IKASVSALKA FPEFNASLDG DNLVLKNYFN 400
IGFAADTPNG LVVPVIKDVD QKGLKQISQE LTELSKKARE GKLKPQEMQG 450
ACFTISSLGG IGGTGFTPIV NAPEVAILGV CKSQIKPVWN GKEFAPRLMC 500
PLSLSFDHRV IDGAAGMRFT VFLAKLLKDF RRITL 535
Length:535
Mass (Da):55,209
Last modified:September 22, 2009 - v1
Checksum:iF05F7CDA19624106
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM889136 Genomic DNA. Translation: CBA06394.1.
RefSeqiWP_015815659.1. NC_013016.1.
YP_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:
EMBL
GenBank
DDBJ
Links Updated
AM889136 Genomic DNA. Translation: CBA06394.1 .
RefSeqi WP_015815659.1. NC_013016.1.
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: alpha14.

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: September 3, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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