Q8NNF6 (Q8NNF6_CORGL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156

Gene names

Name:	aceE EMBL CAF20589.1
Ordered Locus Names:	cg2466, Cgl2248

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	922 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. PIRNR PIRNR000156
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156
Cofactor	Thiamine pyrophosphate By similarity. PIRNR PIRNR000156

Ontologies

Keywords
Ligand	Pyruvate PIRNR PIRNR000156 EMBL BAB99641.1 Thiamine pyrophosphate PIRNR PIRNR000156
Molecular function	Oxidoreductase PIRNR PIRNR000156 EMBL BAB99641.1
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q8NNF6 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 5B949B2A72B855BF	FASTA	922	102,826
	10 20 30 40 50 60 MADQAKLGGK PSDDSNFAMI RDGVASYLND SDPEETNEWM DSLDGLLQES SPERARYLML 70 80 90 100 110 120 RLLERASAKR VSLPPMTSTD YVNTIPTSME PEFPGDEEME KRYRRWIRWN AAIMVHRAQR 130 140 150 160 170 180 PGIGVGGHIS TYAGAAPLYE VGFNHFFRGK DHPGGGDQIF FQGHASPGMY ARAFMEGRLS 190 200 210 220 230 240 EDDLDGFRQE VSREQGGIPS YPHPHGMKDF WEFPTVSMGL GPMDAIYQAR FNRYLENRGI 250 260 270 280 290 300 KDTSDQHVWA FLGDGEMDEP ESRGLIQQAA LNNLDNLTFV VNCNLQRLDG PVRGNTKIIQ 310 320 330 340 350 360 ELESFFRGAG WSVIKVVWGR EWDELLEKDQ DGALVEIMNN TSDGDYQTFK ANDGAYVREH 370 380 390 400 410 420 FFGRDPRTAK LVENMTDEEI WKLPRGGHDY RKVYAAYKRA LETKDRPTVI LAHTIKGYGL 430 440 450 460 470 480 GHNFEGRNAT HQMKKLTLDD LKLFRDKQGI PITDEQLEKD PYLPPYYHPG EDAPEIKYMK 490 500 510 520 530 540 ERRAALGGYL PERRENYDPI QVPPLDKLRS VRKGSGKQQI ATTMATVRTF KELMRDKGLA 550 560 570 580 590 600 DRLVPIIPDE ARTFGLDSWF PTLKIYNPHG QNYVPVDHDL MLSYREAPEG QILHEGINEA 610 620 630 640 650 660 GSVASFIAAG TSYATHGKAM IPLYIFYSMF GFQRTGDSIW AAADQMARGF LLGATAGRTT 670 680 690 700 710 720 LTGEGLQHMD GHSPVLASTN EGVETYDPSF AYEIAHLVHR GIDRMYGPGK GEDVIYYITI 730 740 750 760 770 780 YNEPTPQPAE PEGLDVEGLH KGIYLYSRGE GTGHEANILA SGVGMQWALK AASILEADYG 790 800 810 820 830 840 VRANIYSATS WVNLARDGAA RNKAQLRNPG ADAGEAFVTT QLKQTSGPYV AVSDFSTDLP 850 860 870 880 890 900 NQIREWVPGD YTVLGADGFG FSDTRPAARR FFNIDAESIV VAVLNSLARE GKIDVSVAAQ 910 920 AAEKFKLDDP TSVSVDPNAP EE

References

[1]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 [Kalinowski].
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 [Nakagawa].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB99641.1. BX927154 Genomic DNA. Translation: CAF20589.1.
RefSeq	NP_601447.1. NC_003450.3. YP_226490.1. NC_006958.1.
3D structure databases
HSSP	HSSP built from PDB template 1L8A based on UniProtKB P06958.
ProteinModelPortal	Q8NNF6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1020200. 3344029.
GenomeReviews	Gene locus Cgl2248 in contig BA000036_GR. Gene locus cg2466 in contig BX927147_GR.
KEGG	cgb:cg2466. cgl:NCgl2167.
PATRIC	21496490. VBICorGlu203724_2180.
Phylogenomic databases
HOGENOM	HBG289271.
OMA	FRQEKSH.
PhylomeDB	Q8NNF6.
ProtClustDB	PRK09405.
Enzyme and pathway databases
BRENDA	1.2.4.1. 812.
Family and domain databases
InterPro	IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KO	K00163.
PANTHER	PTHR11624:SF37. PTHR11624:SF37. 1 hit.
Pfam	PF00456. Transketolase_N. 2 hits. [Graphical view]
PIRSF	PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
TIGRFAMs	TIGR00759. AceE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q8NNF6_CORGL

Accession

Primary (citable) accession number: Q8NNF6
Secondary accession number(s): Q6M3J1

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2002
Last sequence update:	October 1, 2002
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)