C6EAU2 (C6EAU2_ECOBD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Dihydrolipoamide acetyltransferase EMBL ACT42015.1
EC=2.3.1.12 EMBL ACT42015.1

Submitted name:
Dihydrolipoamide acetyltransferase / lipoate acetyltransferase, subunit of pyruvate dehydrogenase multienzyme complex EMBL CAQ30630.1
EC=1.2.1.- EMBL CAQ30630.1
EC=2.3.1.12 EMBL CAQ30630.1
Submitted name:
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase EMBL ACT30503.1
EC=2.3.1.12 EMBL ACT30503.1

Gene names

Name:	aceF EMBL ACT42015.1
Ordered Locus Names:	B21_00113, ECBD_3504, ECD_00114

Organism

Escherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]

Taxonomic identifier

469008 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family. RuleBase RU003423 Contains 3 lipoyl-binding domains.

Ontologies

Keywords
Domain	Lipoyl SAAS SAAS003016 RuleBase RU000447
Ligand	Pyruvate EMBL ACT30503.1
Molecular function	Acyltransferase RuleBase RU003765 EMBL ACT30503.1 Oxidoreductase EMBL CAQ30630.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	C6EAU2 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: 802A513A1E88F5DA	FASTA	630	66,096
	10 20 30 40 50 60 MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS 70 80 90 100 110 120 VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV 130 140 150 160 170 180 TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA 190 200 210 220 230 240 GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT 250 260 270 280 290 300 VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 310 320 330 340 350 360 AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED 370 380 390 400 410 420 VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW 430 440 450 460 470 480 VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS 490 500 510 520 530 540 LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA 550 560 570 580 590 600 GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 610 620 630 FDHRVIDGAD GARFITIINN TLSDIRRLVM

References

[1]	"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)." Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F. J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [Korea].
[2]	"Sequencing and gene expression analysis of Escherichia coli BL21." Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M. Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [Austria].
[3]	"Complete sequence of Escherichia coli BL21(DE3)." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E. Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001665 Genomic DNA. Translation: ACT30503.1. CP001509 Genomic DNA. Translation: ACT42015.1. AM946981 Genomic DNA. Translation: CAQ30630.1.
RefSeq	YP_002997980.1. NC_012892.2. YP_003037688.1. NC_012947.1. YP_003052786.1. NC_012971.2.
3D structure databases
SMR	C6EAU2. Positions 1-81, 106-183, 206-284, 326-363, 388-630.
ModBase	Search...
Protein-protein interaction databases
STRING	469008.ECBD_3504.
Proteomic databases
PRIDE	C6EAU2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACT30503; ACT30503; ECBD_3504. ACT42015; ACT42015; ECD_00114. CAQ30630; CAQ30630; B21_00113.
GeneID	8115316. 8157821. 8181520.
KEGG	ebd:ECBD_3504. ebe:B21_00113. ebl:ECD_00114.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281562.
KO	K00627.
OMA	VPMTRLM.
ProtClustDB	PRK11854.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 3 hits. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 3 hits.
TIGRFAMs	TIGR01348. PDHac_trf_long. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 3 hits. PS00189. LIPOYL. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C6EAU2_ECOBD

Accession

Primary (citable) accession number: C6EAU2
Secondary accession number(s): C5W122

Entry history

Integrated into UniProtKB/TrEMBL:	September 1, 2009
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)