ID A0A2V0NTA7_9CHLO Unreviewed; 881 AA.
AC A0A2V0NTA7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=Rsub_02606 {ECO:0000313|EMBL:GBF89902.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF89902.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF89902.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF89902.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF89902.1}.
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DR EMBL; BDRX01000013; GBF89902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0NTA7; -.
DR STRING; 307507.A0A2V0NTA7; -.
DR InParanoid; A0A2V0NTA7; -.
DR Proteomes; UP000247498; 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; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 2.
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; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
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; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 2.
DR SMART; SM00861; 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:UP000247498};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 527..703
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 881 AA; 98359 MW; D15FD3150405D92D CRC64;
MVLGGVYTGM LLKRGQGAGK RLLRGYHASK GVAAAEPEPV PLSKLKDSFN DATSVTYLEE
MEKRYQDDPG SVDRTWASFF KSLESGVPGE AIAEAFDAFE KGESRVSPLA AAAISNQTIQ
ESMRLVMMVR AYQVNGHFAA SLDPLGLDQR PHNPELDPAS YGFSEADMDR EFFIGSWGGT
SGFLSEDRPI RTLREILTRL REAYCGHIGY EYMHIPEREK CNWLRERIET PVEAVFSTKK
KQHTLDRLAW SEMFETFCSN KFTAAKRFGL EGCETLIPGM KALIDRVTDL GVESIVMGMP
HRGRLNVLAN VVRKPMAQIF SEFSGKAQKG AENEYMGSGD VKYHLGTSYN RPTINGKMVH
LSLMANPSHL EAVNTCVLGK TRAKQLLSND DERGKHMGVL LHGDGAFSGQ GIVFETLDMC
GLPDYSTGGT IHLVVNNQVA FTTDPRKSRS SPYCTDVAKA LNCPIFHVNA DDVEAVVRTC
ELAAEWRQRW KTDVVVDLVC YRKYGHNEID EPMFTQPLMY KKIRGHKNAH QRYVEQLLAE
GSLDSAAGNV VRLSGQDVER GTFSHRHATI HDQETGEKYT SLCHVFPGQK PGQLTISNSS
LSEFGVLGFE LGFSMETPNS LTLWEAQFGD FANGAQAGGA LVIFDQFLSS GEAKWLRQSG
LVGPEHSSAR LERFLQMSDE NPYVHRQFRK PLIVMSPKNL LRHPKCKSDL DEFDDVPGDH
GIVGVRFKRV IMDDRGLLPK SRAPRPPQET VVKRVVFCTG KVFYELHAER ERLGVQDDIA
IVRIEQLAPF PFDLVSRELY RYPGAEMVWC QEEPMNMGAY FHIQPRMESC LRAEGRPTTG
RITYAGRPPS ASTATGFGQV HAQEQARLVG EALDLSFKMQ I
//
