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Database: UniProt
Entry: F0YBC0_AURAN
LinkDB: F0YBC0_AURAN
Original site: F0YBC0_AURAN 
ID   F0YBC0_AURAN            Unreviewed;       795 AA.
AC   F0YBC0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=dihydrolipoyllysine-residue succinyltransferase {ECO:0000256|ARBA:ARBA00012945};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032406};
GN   ORFNames=AURANDRAFT_71782 {ECO:0000313|EMBL:EGB07632.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB07632.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|ARBA:ARBA00005145}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; GL833130; EGB07632.1; -; Genomic_DNA.
DR   RefSeq; XP_009037630.1; XM_009039382.1.
DR   AlphaFoldDB; F0YBC0; -.
DR   EnsemblProtists; EGB07632; EGB07632; AURANDRAFT_71782.
DR   GeneID; 20228397; -.
DR   KEGG; aaf:AURANDRAFT_71782; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   InParanoid; F0YBC0; -.
DR   OrthoDB; 672at2759; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004340; F:glucokinase activity; IEA:InterPro.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR003836; Glucokinase.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   NCBIfam; TIGR01347; sucB; 1.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          429..504
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          535..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   795 AA;  82684 MW;  F36C59ED4BDAFF35 CRC64;
     MLTLLPLLAS SFAPPPRVRV VRVAPRRASD LLLIGDVGGT NSRLQLHEMA RSEVAECAFD
     GTGCAAAAAS GKLVSERRYE NARFASFDAV VAQFFRDEAL ADAHLAVVCL AVAGVVKNNA
     CQLTNRDALW RIDGAALDAA LPKGAAKVVL VNDFLGAGYG LLSLDPRDSV DLAPGDADGD
     GPMACLGAGT GLGEVYLTPN LGAEGLGYTA WPTEGGHVDL APRDDEEADL LAWLKARVTG
     GGRVSVERVC SGPGVAHVYA FLAERRAADP GVAAEVAEAD AVGQGARVIG AAAAEGRCDV
     CARAMDIFAS LLGNEAGNAA LKWNPTSGLF LAGGVCVDEN NRRLFRDDGP FMAAYRDRGR
     VSPFLDDIPV RLVTEKDLGL RGAKLLATSI LASANRKAPS AALPRATTWA ARRPGALAPR
     AVAARCFSVE DVPVPSMGDS ITEGTVAEWS VEVGDTVAVD DIVVMIETDK VSVEVRAPVS
     GAVTELLAEL DDVVEVGAPL FKIDTSVEVA AAAPAAAAPA AAAPAAPAAE APAAPAPAAA
     PVPAPTPAPA MPEPPKAAGS RGETRVKMNR MRQRIAERLK EAQNTAACLT TFQECDMGAL
     MELRKAHKDE FEKVHGVKLG FMSAFVAAST KALIEIPAVN AYIDDDAKEI VYRDYCDVSV
     AVASPNGLVV PVLRNTEAMS FADVEKTIGA FGAKARAGAL ALEDMAGGTF TISNGGVFGS
     LMGTPIINPP QSAILGMHAT KMRAVVAKDG SVVARPMMYL ALTYDHRMID GREAVTFLKS
     VANKIEDPAR LLLDI
//
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