ID   G7SQU7_9FLAO            Unreviewed;       908 AA.
AC   G7SQU7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:AER40366.1};
GN   ORFNames=MADAR_041 {ECO:0000313|EMBL:AER40366.1};
OS   Blattabacterium sp. (Mastotermes darwiniensis) str. MADAR.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1074889 {ECO:0000313|EMBL:AER40366.1, ECO:0000313|Proteomes:UP000006133};
RN   [1] {ECO:0000313|EMBL:AER40366.1, ECO:0000313|Proteomes:UP000006133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MADAR {ECO:0000313|EMBL:AER40366.1,
RC   ECO:0000313|Proteomes:UP000006133};
RX   PubMed=22020505; DOI=10.1128/AEM.06540-11;
RA   Sabree Z.L., Huang C.Y., Arakawa G., Tokuda G., Lo N., Watanabe H.,
RA   Moran N.A.;
RT   "Genome shrinkage and loss of nutrient-providing potential in the obligate
RT   symbiont of the primitive termite Mastotermes darwiniensis.";
RL   Appl. Environ. Microbiol. 0:0-0(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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; CP003000; AER40366.1; -; Genomic_DNA.
DR   RefSeq; WP_014158528.1; NC_016146.1.
DR   AlphaFoldDB; G7SQU7; -.
DR   STRING; 1074889.MADAR_041; -.
DR   KEGG; bmm:MADAR_041; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006133; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          573..765
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   908 AA;  106276 MW;  F901D41582033422 CRC64;
     MSDRYSFLND IHNIEFLYKK YKENPNSIEP SWCAFFYGFD FNKESCQIFH EKNNETSIED
     IHKEFSVYNL VQAYRKRGHL FTETNPILKR RKHFPTLDLK NFGLSEKELD LSFEAGKLIG
     IGKTTLRKII DHLKSIYCNS IGIEYMYISD PKKIEWIENW FTRKKLEFSK EKRKFFLQKL
     NEAVAFENFI HTKFVGKKRF SIEGNESLLP ALEEMIEYTS NKYLTEDFVI GMSHRGRLNI
     LSNFFRKNYS NIFSEFQEKK YKEESFSGDV KYHLGFTKFR KTCKGRYIKM SLVPNPSHLE
     SVNPIVEGIT RSKIDINYNG NSDSKKIIPI LIHGDAALSG QGIVYEVIQL SKLKGYKTGG
     TIHIVINNQI GFTTNYTEGR SSIYCTDIAK VLLSPVLHIN ADDIESVIRA IHFAVDFRMH
     YHEDVFIDLL GYRKYGHNEG DEPRFTQPTL YKVISKHTNS YNLYKRKLEK EGTINSIFIQ
     KMEKKYEDIL NRGYEEAKTM KWNVINSFLK EEWKNFPIIN NNEIFQKVNT QFPINRLIEI
     ANRIFTLPMD KKFFSKTKFI FKKRLEMVKN QLLDWSMAEL LSYGTLLDEG YHIRLSGEDV
     ARGTFSQRHA ILKTEEDEEI ISLNNIRVGQ GKMQVYNSPL SEYGVLGFDY GYAMFSPYTL
     TLWEAQFGDF GNGGQIIIDQ YISSGEDKWK IRNGMVMLLP HGYEGQGPEH SSARIERYLQ
     LCANNNLFIV NCTTPANFYH LLRRQMKLKF RKPLLVFTPK SLLRHIKCKS TMKELSEGEF
     QEILDDVSVI DVDKVTRLIF CSGKIYYDLL NKKESIKDEK TALIRIEQIY PLKEKKIIEL
     FNKYKNKKIV LWVQEEPENM GLWSFILRKI SSISFNLIAP SERSSPSTGS YTNFLKIQNK
     ILDRAFIS
//