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};
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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
//
