Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

SELMODRAFT_121442

Organism
Selaginella moellendorffii (Spikemoss)
Status
Unreviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • (R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
ORF Names:SELMODRAFT_121442Imported, SELMODRAFT_94277Imported
OrganismiSelaginella moellendorffii (Spikemoss)Imported
Taxonomic identifieri88036 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiidaeSelaginellalesSelaginellaceaeSelaginella
ProteomesiUP000001514: Unassembled WGS sequence

Subcellular locationi

Mitochondrion matrix UniRule annotation

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 1 lipoyl-binding domain.UniRule annotation

Keywords - Domaini

LipoylUniRule annotation

Phylogenomic databases

InParanoidiD8RIN1.
KOiK00627.
OMAiCIPTTIT.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D8RIN1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLFLSILCL TDHVFFSCLV PSHQPLGMPS LSPTMTQGNI VKWKKKEGDK
60 70 80 90 100
VTAGDVLCEI ETDKATVDME CMEDGYLAKI VFSDGAKDIK VGQIIAITVE
110 120 130 140 150
EQGDIDKFKD YKADAPAAPP KPAPKESPPP PKPTESPKPA PSPKPAPAAS
160 170 180 190 200
GDRIIASPNA RKYAQDNQIS LSGVAGTGPG GRIVRADLLI VVFIGGQQVQ
210 220 230 240 250
EPRRAETPGD STSLDYTDLP NTQIRRVIAQ RLLQSKQTIP HYYLTVDVRV
260 270 280 290 300
DKLLALRTQL NAKLEKEKRK KLSVNDFVLK AAALALKKVP ECNSSWTDEF
310 320 330 340 350
IRQFHNINIS VAVQTERGLM VPVVKDADKK GLGAISDDVR TLAEKARENT
360 370 380 390 400
LKPSDYDGGT FTVSNLGGPF GIKQFCAIIN PPQSCILAVG TTDKRVIPGE
410 420 430 440
NDGEYTAATF MSATLSCDHR VVDGAIGAHW LGAFKGYIED PMTLLL
Length:446
Mass (Da):48,348
Last modified:October 5, 2010 - v1
Checksum:iC3C1AEEA63F986D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377630 Genomic DNA. Translation: EFJ13978.1.
GL377580 Genomic DNA. Translation: EFJ28117.1.
RefSeqiXP_002970791.1. XM_002970745.1.
XP_002985103.1. XM_002985057.1.
UniGeneiSmo.15286.
Smo.2571.

Genome annotation databases

EnsemblPlantsiEFJ13978; EFJ13978; SELMODRAFT_121442.
EFJ28117; EFJ28117; SELMODRAFT_94277.
GeneIDi9641347.
9648948.
KEGGismo:SELMODRAFT_121442.
smo:SELMODRAFT_94277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377630 Genomic DNA. Translation: EFJ13978.1.
GL377580 Genomic DNA. Translation: EFJ28117.1.
RefSeqiXP_002970791.1. XM_002970745.1.
XP_002985103.1. XM_002985057.1.
UniGeneiSmo.15286.
Smo.2571.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEFJ13978; EFJ13978; SELMODRAFT_121442.
EFJ28117; EFJ28117; SELMODRAFT_94277.
GeneIDi9641347.
9648948.
KEGGismo:SELMODRAFT_121442.
smo:SELMODRAFT_94277.

Phylogenomic databases

InParanoidiD8RIN1.
KOiK00627.
OMAiCIPTTIT.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Selaginella genome identifies genetic changes associated with the evolution of vascular plants."
    Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., Chapple C., Cheng C.
    , Correa L.G., Dacre M., DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.
    Science 332:960-963(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiD8RIN1_SELML
AccessioniPrimary (citable) accession number: D8RIN1
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: January 7, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.