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Database: UniProt
Entry: G1KT20_ANOCA
LinkDB: G1KT20_ANOCA
Original site: G1KT20_ANOCA 
ID   G1KT20_ANOCA            Unreviewed;       522 AA.
AC   G1KT20;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000256|ARBA:ARBA00020294};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|ARBA:ARBA00032406};
DE   AltName: Full=E2K {ECO:0000256|ARBA:ARBA00031331};
GN   Name=DLST {ECO:0000313|Ensembl:ENSACAP00000016485.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016485.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000016485.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000016485.3,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000016485.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   -!- SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of OGDH
CC       (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide
CC       succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3).
CC       It contains multiple copies of the three enzymatic components (E1, E2
CC       and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex
CC       associates with KAT2A. {ECO:0000256|ARBA:ARBA00038837}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   RefSeq; XP_003214492.2; XM_003214444.3.
DR   AlphaFoldDB; G1KT20; -.
DR   STRING; 28377.ENSACAP00000016485; -.
DR   Ensembl; ENSACAT00000016811.4; ENSACAP00000016485.3; ENSACAG00000016718.4.
DR   GeneID; 100553287; -.
DR   KEGG; acs:100553287; -.
DR   CTD; 1743; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   GeneTree; ENSGT00930000151014; -.
DR   HOGENOM; CLU_016733_0_2_1; -.
DR   InParanoid; G1KT20; -.
DR   OrthoDB; 672at2759; -.
DR   TreeFam; TF314164; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001646; Chromosome 1.
DR   Bgee; ENSACAG00000016718; Expressed in heart and 13 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
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   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:UP000001646};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          139..213
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          31..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  55578 MW;  BC81618ACB5032D1 CRC64;
     MAESPSLFRA WPVPPSSPCC PEVVRPSPPF PSSRAHLVAP RPHPASAGPG SGARPGPQAA
     AAAAMLFLSL ARARCFSRLL GRSLCAPRQG NCPQGKRSLS GVSRCQGLAY ANSRKHLVNS
     SRVFTVRYFR STAACREEVV TVNTPAFAES VTEGDVRWEK AVGDTVAEDE VVCEIETDKT
     SVQVPAPAAG VIEALLVPDG GKVEGGTPLF KLRKGGAAPA KAKPAAAPAP EPAAAPAPPI
     APAAPIPTAM PPVPPVSAVP VDAKPVSAVK PTAAPAAAPA EPGVSKGARL EQRVKMNRMR
     QRIAQRLKEA QNTCAMLTTF NEIDMSNIQE MRARHRDSFL KKHNMKLGFM SAFVKASAFA
     LQEQPVVNAV IDDTTKEIVY REYVDISVAV ATPRGLVVPV IRNVDTMNFA DIERAINELG
     EKARKNELAI EDMDGGTFTI SNGGVFGSLF GTPIINPPQS AILGMHGIFD RPVAIGGKVE
     VRPMMFVALT YDHRLIDGRE AVTFLRKIKA VVEDPRVLLL DL
//
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