ID   C1DB59_LARHH            Unreviewed;       939 AA.
AC   C1DB59;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=kgd {ECO:0000313|EMBL:ACO75398.1};
GN   OrderedLocusNames=LHK_02416 {ECO:0000313|EMBL:ACO75398.1};
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75398.1, ECO:0000313|Proteomes:UP000002010};
RN   [1] {ECO:0000313|EMBL:ACO75398.1, ECO:0000313|Proteomes:UP000002010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75398.1,
RC   ECO:0000313|Proteomes:UP000002010};
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA   Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA   Pallen M.J., Lok S., Yuen K.Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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};
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DR   EMBL; CP001154; ACO75398.1; -; Genomic_DNA.
DR   RefSeq; WP_012697884.1; NC_012559.1.
DR   AlphaFoldDB; C1DB59; -.
DR   STRING; 557598.LHK_02416; -.
DR   KEGG; lhk:LHK_02416; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   Proteomes; UP000002010; Chromosome.
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; 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   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; 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; 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:ACO75398.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          593..790
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   939 AA;  105248 MW;  9E450A1D333BE37B CRC64;
     MMQAAISHSY LFGGNAPFIE ELYEQYLDDP ATVSAEWREY FDKLQQTGGA TRDVPHQPIQ
     ESFIQLAKTP RVFVNKPSEA TWEAMQKQVA VLKLISAYRV LGSRWATLDP LKRMDTQPVP
     ELDPAYHGLT DTDMAQVFNT GSFVGLASGS LSEILGTLKQ TYCGNIGLEY MHIIDSKQKR
     WVQNYFEGSR STPRYDAAKK RSILKQVTAA ETLERYLHTK YVGQKRFSLE GGESMIAALD
     HLIQNATGFG VKELIVGMAH RGRLNVLVNT LGKLPRDLFS EFEGRPAVEL PSGDVKYHMG
     YSSDIPTQNG PMHVSLAFNP SHLEIVNPVV EGSVRARQQR RRDTERREVV PVLIHGDAAF
     GGLGVNQGTF NLSGTRGYGT GGTLHFVVNN QIGFTTSDTR DMRSSMYATD IAKMVDAPIF
     HVNGDDPEAV CFVMQAALEF RMQFKKDVVV DMVCFRKLGH NEGDDPMLTQ PMMYKKIVQH
     PGVRARYVER LVQEGSIDAS EADSLISAYR AALDKGEHVE QTVLSNYTRE FKLDWTPYIG
     THWAHPTDTT LPTADLQRLA DKLTTVPEGF KLHPTVSKLL AARREMAAGN QAVDWGMAET
     LAYASLVESG YGVRLSGEDS GRGTFSHRHS VLHDQNRERW DAGAYVPLRN LSDNQAEFLV
     IDSILNEEAV LAYEYGYACS SPKELTIWEA QFGDFANGAQ VAIDQFIVSG ETKWGRLCGL
     TMILPHGYDG QGPEHSSARV ERYLQLCAEH NVQVVMPSTA AQMFHVLRRQ MLRPYRKPLI
     IPMSKRLLRY KESMSPLADF TSGGFKPVIG EIEALDAKKV KRVVLCAGQV YYDLLNARRE
     RDIQDIAIVR VEQLYPFPTE QLAAELAQYT NARELMWVQE EPKNQGAWYQ IRHRLERQLA
     PKQTLLFAGR PSSASPAVGY MSKHVAQLKA FLEEAMTLG
//