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Database: UniProt
Entry: I3Z3Z6_BELBD
LinkDB: I3Z3Z6_BELBD
Original site: I3Z3Z6_BELBD 
ID   I3Z3Z6_BELBD            Unreviewed;       932 AA.
AC   I3Z3Z6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Belba_1340 {ECO:0000313|EMBL:AFL83964.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL83964.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP003281; AFL83964.1; -; Genomic_DNA.
DR   RefSeq; WP_014771960.1; NC_018010.1.
DR   AlphaFoldDB; I3Z3Z6; -.
DR   STRING; 866536.Belba_1340; -.
DR   KEGG; bbd:Belba_1340; -.
DR   PATRIC; fig|866536.3.peg.1386; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006050; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000006050};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          596..789
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   932 AA;  105991 MW;  B32F939FB83F4E73 CRC64;
     MDKYSYIANA HVAYIDELYA EYKNNPESVD PSWKTFFDGF EFAITQYGED ENGGAQVTNI
     SSSQPAANGS LATRGTIMDM EQLPKEIKVR ALIHAHRSRA HLRSKTNPVR ERRDRKALID
     LEDFGLDQND LNTEFQAGNE IGIGAAKLSK IIESLKTIYE GPMGFEYLYI RDPEMLDWLK
     TKIEKEALSF NPPTEEKKRI LSKLNEAVVF ENFLHTKYLG QKRFSLEGGE STIPFLDAVI
     NKGAQLGVEE VMIGMAHRGR LNVLANIMGK TYEQIFSEFE GTAKPDLTMG DGDVKYHMGY
     SSDITTQDDK KVNLKLAPNP SHLEAVNPVV EGFIRAKIDS QHQGDSTKAL PILIHGDAAV
     AGQGIVYEVT QMAGLKGYNT GGTIHFVINN QVGFTTDFDD ARSSIYCTDV AKIIDAPVIH
     VNGDDAEAVV FAARLAAEFR QKFRKDIFID MVCYRRHGHN ESDEPKFTQP ELYNIISKHS
     NPREIYVKRL SERGDLDAKI AKQMDAEFRQ LLQDRLNMVK EKPLPYQFTK FEKEWQSLRR
     STPEDFEQSP DTSISQDFIE KVADAITHVP KGFKPIKQID IQLKQRKDMF FNAKSLNWAS
     AELLAYGSLL LEGKTVRLTG QDVQRGTFSH RHAVVHDSTT NKPYNFLKEM KDSKGQFSIY
     NSLLSEYAVL GFEYGYAMAS PNSLAIWEAQ FGDFANGAQT MIDQFISSGE SKWQKMNGLV
     MLLPHGYEGQ GPEHSNARPE RFLQLSAEYN MVVANITEPS NFFHLLRRQM AWEFRKPCIV
     MSPKSLLRHP KVVSPIEEFT SGSFREIILD NTVKAKDVRR VLLCSGKIYY DLEEMREKEK
     VKDVAIIRIE QLHPLPKKQM TEALKAYKDA EIVWVQEEPE NMGYWNYILR MLYKELPMDV
     IARKMSASPA TGYNKVHVEE QLNIVKKALK LS
//
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