ID A7TA13_NEMVE Unreviewed; 659 AA.
AC A7TA13;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=NEMVEDRAFT_v1g151912 {ECO:0000313|EMBL:EDO27159.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO27159.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO27159.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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DR EMBL; DS473757; EDO27159.1; -; Genomic_DNA.
DR RefSeq; XP_001619259.1; XM_001619209.1.
DR AlphaFoldDB; A7TA13; -.
DR STRING; 45351.A7TA13; -.
DR EnsemblMetazoa; EDO27159; EDO27159; NEMVEDRAFT_v1g151912.
DR KEGG; nve:5497427; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_2_2_1; -.
DR InParanoid; A7TA13; -.
DR OMA; YMHINDP; -.
DR PhylomeDB; A7TA13; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 5..42
FT /note="2-oxoglutarate dehydrogenase E1 component N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16078"
FT DOMAIN 194..509
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT DOMAIN 584..659
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
SQ SEQUENCE 659 AA; 74437 MW; 4783BF478A046351 CRC64;
MDRFSFLNAA HTAFFADLYD QYLQNPDTVE PSWRSFFQGF DFASEFSSPV EQLSAIASGG
ATVNENAEKL QKEFNVLKLI EGYRTRGHLF TKTNPVRERR TYSPTLAIEN FGLSQSDLTT
VFDAAKLVNM QPSTLADIIK HLESVYCSSI GIEYMYIRDP KVQEWIKNRL DVNDNQPQFS
TDKKKNILKK LNEAVSFETF LHTKYVGQKR FSLEGCESAI PALDALIEGA AERGVEQFVM
GMAHRGRLNV LANIFGKNTQ NIFSEFDGKD YDDDMYFDGD VKYHLGLTSD RTTTSGKKIN
LNLAPNPSHL ETVGAVIEGI ARAKQDRNYP NDFSKVLPIA VHGDAAIAGQ GIVYEIIQMA
KLDGYKTGGT IHLVINNQVG FTTNYLDARS STYCTDVAKV TLSPVLHVNA DDAEAVVHAM
LFALDYRMEF GSDVFIDLLG YRKYGHNEGD EPKFTQPILY KTIAKHKNAR DIYAEKLKAA
GVIDANYVKE LEEKYKSDLD ENLEESRKKD LTVITPFMQN EWTGFEQVSD DGMLKKVDTS
FDKDKLTEIA KTITELPSDK KFISKISKII NARKEMYFET NQLYWEMGEL LAYGSLLAEG
YDVRISGQDV ERGTFSHRHA VVKVEASEEE VILLNDIKDK KGNFYIYNSH LSEYGVVGF
//
