Q0SHG3 (Q0SHG3_RHOSR) 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:	aceE1 EMBL ABG93023.1
Ordered Locus Names:	RHA1_ro01197

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL ABG93023.1

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	951 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 ABG93023.1 Thiamine pyrophosphate PIRNR PIRNR000156
Molecular function	Oxidoreductase PIRNR PIRNR000156 EMBL ABG93023.1
Technical term	Complete 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)
	Q0SHG3 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: DDB2278AD0BBF56C	FASTA	951	104,601
	10 20 30 40 50 60 MSDLIQGPAS QPDSATPGAG AAQPSNPSAT PGSDARVRVI REGVASYLPD IDPDETTEWL 70 80 90 100 110 120 ESFDGLLDRS GPTRARYLML RMLERAGEKH VALPALTSTD YVNTIPTENE PWFPGDEETE 130 140 150 160 170 180 RRYRAFIRWN AAVMVTRAQR PGVGVGGHIS TYASSAALYE VGFNHFFRGK DHPGGGDQIF 190 200 210 220 230 240 IQGHASPGIY ARAFLEGRIP AERMDGFRQE HSHADQGGGL PSYPHPRLLP DFWEFPTVSM 250 260 270 280 290 300 GLGPMNAIYQ ARFNHYLHDR GIKDTADQHV WAFLGDGEMD EPESRGLAHV AATEGLDNLT 310 320 330 340 350 360 FVVNCNLQRL DGPVRGNGKI IQELESFFRG AGWNVIKVVW GREWDALLHA DRDGALVNLM 370 380 390 400 410 420 NVTPDGDYQT YKANDGGYVR EHFFGRDPRT KELVANLSDQ DIWNLKRGGH DYRKIYAAYA 430 440 450 460 470 480 AAMAHKGQPT VILAHTIKGY TLGKHFEGRN ATHQMKKLTL DDLKNFRDLQ RIPISDAELE 490 500 510 520 530 540 KDPKMPPYYH PGPDAPEIQY MLDRRRALGG FLPQRRTSPA PLPMPPDSTY DVVRKGSGKQ 550 560 570 580 590 600 QVATTMALVR IMKELLRDKE IGKRIVPIIP DEARTFGMDS WFPSLKIYNR NGQLYTAVDA 610 620 630 640 650 660 DLMLAYKESE IGQILHEGIN EAGSTASFTA VGTSYATHGE PMIPLYIFYS MFGFQRTGDG 670 680 690 700 710 720 LWAAADQMAR GFVLGATAGR TTLTGEGLQH ADGHSLLLAS TNPAAVAYDP AFSYEIAHIV 730 740 750 760 770 780 KDGLRRMYGG TDGVDGFGGE DIFYYITLYN EPYSQPAEPA DLNVDGLLKG MYLFKKSQAS 790 800 810 820 830 840 GPKAQILVSG VTMPEGLRAQ ELLADEWGVA ADVWSVTSWG ELRRDGIESE RQALRDPGTD 850 860 870 880 890 900 APLPYVTQAL SDAAGPFVAA SDWMRAVADQ IRQWVPGSYT TLGTDGFGFS DTRPAARRYF 910 920 930 940 950 NVDAESIVVA VLSALAGEGT LDRSKAVEAA NRYRIDDVRA AAVSYTDTGS A

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG93023.1.
RefSeq	YP_701181.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0SHG3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0SHG3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4219318.
GenomeReviews	Gene locus RHA1_ro01197 in contig CP000431_GR.
KEGG	rha:RHA1_ro01197.
PATRIC	23201211. VBIRhoJos26306_1224.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2609.
HOGENOM	HBG289271.
OMA	FRQEKSH.
PhylomeDB	Q0SHG3.
ProtClustDB	PRK09405.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO01197-MONOMER.
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. 1 hit. [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

Q0SHG3_RHOSR

Accession

Primary (citable) accession number: Q0SHG3

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)