ID   A0A418NXT0_9SPHN        Unreviewed;       945 AA.
AC   A0A418NXT0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=D2V07_02765 {ECO:0000313|EMBL:RIV89406.1};
OS   Aurantiacibacter zhengii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV89406.1, ECO:0000313|Proteomes:UP000286576};
RN   [1] {ECO:0000313|EMBL:RIV89406.1, ECO:0000313|Proteomes:UP000286576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V18 {ECO:0000313|EMBL:RIV89406.1,
RC   ECO:0000313|Proteomes:UP000286576};
RA   Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA   Xu X.-W.;
RT   "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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:RIV89406.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QXFL01000001; RIV89406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418NXT0; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000286576; 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; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:RIV89406.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286576};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          585..776
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  105183 MW;  EAA451EAA3637F77 CRC64;
     MGKEPDNFLP ELPPQEGAQP GPSWGNPRWP LTDDAGGWSQ AMDPTDMVAV VKQSAAKAGK
     PTDAASIEAA ARDSIQAMLL IRLYRVRGHL AAKLDPLGLS HTAEPEELSL AWHGFAGQED
     KEVYVGGAFG FDWVKVGDLY DALRITYCGH VGLEYMHIAD TEERRFLQDR FESPEETIQF
     TPEGKKAILQ AVIRGEEYEK YLAKKYVGTK RFGLDGGESM IPALEAVIKY GGALGVREII
     YGMAHRGRLN VLANVMAKPY KVIFHEFSGG SSNPDDVGGS GDVKYHLGTS TDREFDGIKV
     HMSLVPNPSH LEAVDPVVLG KTRAQQAFRD DLDNHEQVLP VLIHGDAAFA GQGVVWECFG
     LSGVRGYNTG GCIHFVINNQ IGFTTSPKFA RSSPYPSDVA KGVQAPILHV NGDDPEAVTF
     ACKLAIEYRQ TFKRDIVIDM WCYRRFGHNE GDEPKFTQPL MYDEIKSHPR VSEIYSERLK
     SEGVLEEGTA PEIRSQFIAH LDEQFEAAKT YKPNEIDWFA GRWSGLHKPA DPESARRNAE
     TGIEKKLFDS LGRTLTTVPD DLDIHKTLGR VLDAKREMFK TGEGFDWATA EALAFGSLVT
     EGFGVRLSGQ DSGRGTFSQR HAIWVDQNSE EKYVPLAALP HGKFEVYDST LSEFGVLGFE
     YGFALADPKT LVLWEAQFGD FANGAQVMID QFIAAGEVKW QRANGLVMLL PHGYEGQGPE
     HSSARLERFL QLCANDNIQV CNITSPANYF HVLRRQMLRP FRKPLIIMSP KSLLRHPKAK
     SEASLFQTDS HFRRILSDET EIEDSKVRRL VLCSGKVAYD LMEKRDEEGV DDVSIVRIEQ
     LYPFPGEPLA VRMKRMTNLE EVVWCQEEPH NNGAWFFVQN RIEDALTAAG HDGMRPRYAG
     REEAASPATG YAKRHQAQQE ALVSVALGLS ERGKTAASRK TRNTN
//