ID   A8Z634_KARMG            Unreviewed;       904 AA.
AC   A8Z634;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:ABS30585.1};
GN   OrderedLocusNames=SMGWSS_186 {ECO:0000313|EMBL:ABS30585.1};
OS   Karelsulcia muelleri (strain GWSS) (Sulcia muelleri).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Candidatus Karelsulcia.
OX   NCBI_TaxID=444179 {ECO:0000313|EMBL:ABS30585.1, ECO:0000313|Proteomes:UP000000781};
RN   [1] {ECO:0000313|EMBL:ABS30585.1, ECO:0000313|Proteomes:UP000000781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS {ECO:0000313|EMBL:ABS30585.1,
RC   ECO:0000313|Proteomes:UP000000781};
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an ancient
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000770; ABS30585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8Z634; -.
DR   STRING; 444179.SMGWSS_186; -.
DR   KEGG; smg:SMGWSS_186; -.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   Proteomes; UP000000781; 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   Reference proteome {ECO:0000313|Proteomes:UP000000781};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          570..762
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   904 AA;  106507 MW;  002683A6DE104E19 CRC64;
     MDRYSFLNTI NHQQIEILYK KYLEDPDSIE HSWRAFFQGF DFYKEKYTYF CNCKFIKKKK
     SIDTFKEINV LKLINFYKKE GHLFAKINPI SEKIDYPTLN KFFLEKEDID KIFVSSKEIG
     LPPCTLREII FFLKKKYCES IGLEYMYLYN PEQINWINNW INNNNILYNN EKFKILININ
     KATKFENFIH TKFVGQKRFS IEGNESILPA INYIIEYSSI NYSIKDFVIG MSHRGRLNIL
     CNILKKNCKK IFSEFFGKEY IEKKFLGDVK YHLGDNIYIK NKIGREIHIM NVPNSSHLES
     VSPIVEGIVR AKIDNDYNCN LNKVIPILIH GDAAFSAQGI AYEVIQMSLL EGYKTGGTIH
     IIVNNQIGFT TNCSDSRSSI YCTDLAKVIL SPVIHVNSDD VESVIYSIRF AIDFRMSYNK
     DVFVDLLGYR KYGHNEGDDP RFTQPNFYKI IDNNKNLYFI YKNKLKKNKL IYKNKIKFYE
     KKYKNYLNNG FIKSKFEIKT KLDNFLIYKE KLNSANYKVL INEVKTTFKK NILLKIGNKI
     YNVPKNKKFY NKTVKFLKIK KKKLLKKETV DWGIAELLAY GSLLYEGYNI RLSGEDVERG
     TFAHRHIVII SEFEEKIYLL NNIRNGQGKL YVYNSLLSEY GVLGFEYGYS MFNTNTLTLW
     EAQFGDFSNS AQIIIDQYLS SAETKWKIKN GIVLLLPHGE EGQGSEHSSS RIERYLQLCA
     NYNMFICNCS TPSNFYHLLR RQIKFCFIKP LIIFTPKSLL RNIQCISSLS ELSNGKFEEF
     IDDKYVIKNY VDTLVFCSGK IYYDIFKKRK ILNKKNLAII RIEQLYPIIN NLFEKILIQY
     TNKRKIIWVQ EEPENMGVWP YLFRKYSKIP WILISPPESS APSIGRNNFF LKNYLKLINK
     VFNT
//