Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6S7H7 (C6S7H7_NEIML) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Acetyltransferase component of pyruvate dehydrogenase complex RuleBase RU361137

EC=2.3.1.12 RuleBase RU361137
Gene names
Name:aceF EMBL CBA06394.1
Ordered Locus Names:NMO_1180 EMBL CBA06394.1
OrganismNeisseria meningitidis (strain alpha14) [Complete proteome] [HAMAP] EMBL CBA06394.1
Taxonomic identifier662598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity. RuleBase RU361137

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. RuleBase RU361137

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. RuleBase RU361137

Binds 2 lipoyl cofactors covalently By similarity. RuleBase RU361137

Binds 3 lipoyl cofactors covalently By similarity. RuleBase RU361137

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. RuleBase RU361137

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family. RuleBase RU361137

Contains 2 lipoyl-binding domains. RuleBase RU361137

Ontologies

Sequences

Sequence LengthMass (Da)Tools
C6S7H7 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: F05F7CDA19624106

FASTA53555,209
        10         20         30         40         50         60 
MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA DAAGVVKEVK 

        70         80         90        100        110        120 
VKVGDKISEG GVILTVETGA AAAEAASAAA EAQPAPAAAP VAAGGATVQV AVPDIGGHTD 

       130        140        150        160        170        180 
VDVIAVEIKV GDTVAEDDTL ITLETDKATM DVPCTAAGVV KAVFLKVGDK VSEGSAIIEV 

       190        200        210        220        230        240 
ETVGSAAAAP AQAAQAAAPA AAPPPTAAAA PAAAPAPSAP AAAKIDEAAF AKAHAGPSAR 

       250        260        270        280        290        300 
KLARELGVDL GQVKGTGLKG RIVGDDIKAF VKSVMQGGAA KPAAAGASLG SGLDLLPWPK 

       310        320        330        340        350        360 
VDFSKFGNVE VKELSRIKKI SGQNLSRNWV VIPHVTVHEE ADMTELEEFR KQLNKEWERE 

       370        380        390        400        410        420 
GVKLSPLAFI IKASVSALKA FPEFNASLDG DNLVLKNYFN IGFAADTPNG LVVPVIKDVD 

       430        440        450        460        470        480 
QKGLKQISQE LTELSKKARE GKLKPQEMQG ACFTISSLGG IGGTGFTPIV NAPEVAILGV 

       490        500        510        520        530 
CKSQIKPVWN GKEFAPRLMC PLSLSFDHRV IDGAAGMRFT VFLAKLLKDF RRITL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM889136 Genomic DNA. Translation: CBA06394.1.
RefSeqYP_003083358.1. NC_013016.1.

3D structure databases

ProteinModelPortalC6S7H7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING662598.NMO_1180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBA06394; CBA06394; NMO_1180.
GeneID8222195.
KEGGnmi:NMO_1180.
PATRIC20369083. VBINeiMen141067_1500.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281562.
KOK00627.
OMATEIMVAV.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycNMEN662598:GJMX-1173-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6S7H7_NEIML
AccessionPrimary (citable) accession number: C6S7H7
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)