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O59816

- ODP2_SCHPO

UniProt

O59816 - ODP2_SCHPO

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Protein
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Gene
lat1, SPCC794.07
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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).

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei456 – 4561 Reviewed prediction
Active sitei460 – 4601 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: PomBase
Complete GO annotation...

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_215777. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name:
PDC-E2
Short name:
PDCE2
Gene namesi
Name:lat1
ORF Names:SPCC794.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome III

Organism-specific databases

PomBaseiSPCC794.07.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828Mitochondrion By similarity
Add
BLAST
Chaini29 – 483455Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
PRO_0000020482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941N6-lipoyllysine By similarity

Proteomic databases

MaxQBiO59816.
PaxDbiO59816.

Interactioni

Protein-protein interaction databases

BioGridi275378. 8 interactions.
MINTiMINT-4676403.
STRINGi4896.SPCC794.07-1.

Structurei

3D structure databases

ProteinModelPortaliO59816.
SMRiO59816. Positions 58-134, 250-483.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 12875Lipoyl-binding
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiMSMKEGT.
OrthoDBiEOG7TTQJ2.
PhylomeDBiO59816.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59816-1 [UniParc]FASTAAdd to Basket

« Hide

MLSANMLRRM HHGVAVTRML LVSNGKVQVK KSALYPVMAK LARTYATKNY    50
PAHTVINMPA LSPTMTTGNI GAFQKKIGDK IEPGDVLCEI ETDKAQIDFE 100
QQDEGYLAKI LIETGTKDVP VGKPLAVTVE NEGDVAAMAD FTIEDSSAKE 150
PSAKSGEEKS APSSEKQSKE TSSPSNVSGE ERGDRVFASP LARKLAEEKD 200
LDLSQIRGSG PNGRIIKVDI ENFKPVVAPK PSNEAAAKAT TPAASAADAA 250
APGDYEDLPL SNMRKIIASR LAESKNMNPH YYVTVSVNME KIIRLRAALN 300
AMADGRYKLS VNDLVIKATT AALRQVPEVN AAWMGDFIRQ YKNVDISMAV 350
ATPSGLITPV IRNTHALGLA EISTLAKDYG QRARNNKLKP EEYQGGTFTI 400
SNLGMFPVDQ FTAIINPPQA CILAVGTTVD TVVPDSTSEK GFKVAPIMKC 450
TLSSDHRVVD GAMAARFTTA LKKILENPLE IML 483
Length:483
Mass (Da):52,061
Last modified:August 1, 1998 - v1
Checksum:i7E4B6340665932F4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329672 Genomic DNA. Translation: CAA19134.1.
PIRiT41615.
RefSeqiNP_587755.1. NM_001022748.2.

Genome annotation databases

EnsemblFungiiSPCC794.07.1; SPCC794.07.1:pep; SPCC794.07.
GeneIDi2538797.
KEGGispo:SPCC794.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329672 Genomic DNA. Translation: CAA19134.1 .
PIRi T41615.
RefSeqi NP_587755.1. NM_001022748.2.

3D structure databases

ProteinModelPortali O59816.
SMRi O59816. Positions 58-134, 250-483.
ModBasei Search...

Protein-protein interaction databases

BioGridi 275378. 8 interactions.
MINTi MINT-4676403.
STRINGi 4896.SPCC794.07-1.

Proteomic databases

MaxQBi O59816.
PaxDbi O59816.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPCC794.07.1 ; SPCC794.07.1:pep ; SPCC794.07 .
GeneIDi 2538797.
KEGGi spo:SPCC794.07.

Organism-specific databases

PomBasei SPCC794.07.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
KOi K00627.
OMAi MSMKEGT.
OrthoDBi EOG7TTQJ2.
PhylomeDBi O59816.

Enzyme and pathway databases

Reactomei REACT_215777. Pyruvate metabolism.

Miscellaneous databases

NextBioi 20799979.
PROi O59816.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiODP2_SCHPO
AccessioniPrimary (citable) accession number: O59816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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