ID   A0A0P9CSF0_9CHLR        Unreviewed;       375 AA.
AC   A0A0P9CSF0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=2-oxoglutarate dehydrogenase {ECO:0000313|EMBL:KPV48952.1};
DE   Flags: Fragment;
GN   ORFNames=SE17_35315 {ECO:0000313|EMBL:KPV48952.1};
OS   Kouleothrix aurantiaca.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Kouleothrix.
OX   NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV48952.1, ECO:0000313|Proteomes:UP000050509};
RN   [1] {ECO:0000313|EMBL:KPV48952.1, ECO:0000313|Proteomes:UP000050509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM-B {ECO:0000313|EMBL:KPV48952.1,
RC   ECO:0000313|Proteomes:UP000050509};
RA   Hemp J.;
RT   "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KPV48952.1}.
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DR   EMBL; LJCR01002285; KPV48952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9CSF0; -.
DR   PATRIC; fig|186479.3.peg.4475; -.
DR   Proteomes; UP000050509; 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   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
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   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050509};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          4..245
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          227..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPV48952.1"
FT   NON_TER         375
FT                   /evidence="ECO:0000313|EMBL:KPV48952.1"
SQ   SEQUENCE   375 AA;  41077 MW;  FAF0ACBBE7A0B7F3 CRC64;
     GSVGWAGDVK YHLGAQRTYR ESGIDAMPIT LAPNPSHLEF VNPVVEGRAR AAQEKRDRPG
     APEQSDKASL AILLHGDAAF PGQGVVAETL NMSRLIGYRT GGTIHIITNN QIGFTTEPSD
     SRSTLYASDL AKGFEVPIVH VNADDVEACI AVARMAYAYR ETFGRDFVID LVGYRRWGHN
     EGDEPAFTQP TMYAKIATHP TVRQIWAERM AEVGLVSAEE AAQMQADVTE RLQEARREAE
     TKPHEDRRPK PAPPGLARNA HTAVAAEKLQ AMNAALLNRP AGFTINNRLE RTLERRRTAF
     DQANAIDWGH AEALAFASIL ADGVPIRLTG QDSERGTFSH RHAVLRDSTT GQTYTPLPRL
     PHAKASFAIY NSPLS
//