ID A0A1D8AWL1_9BACT Unreviewed; 923 AA.
AC A0A1D8AWL1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:AOS45279.1};
GN ORFNames=Verru16b_02358 {ECO:0000313|EMBL:AOS45279.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS45279.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS45279.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS45279.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-2016) 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; CP016094; AOS45279.1; -; Genomic_DNA.
DR RefSeq; WP_069962447.1; NZ_CP016094.1.
DR AlphaFoldDB; A0A1D8AWL1; -.
DR STRING; 1838286.Verru16b_02358; -.
DR KEGG; obg:Verru16b_02358; -.
DR PATRIC; fig|1838286.3.peg.2369; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000095228; 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 ECO:0000313|EMBL:AOS45279.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 586..779
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 502..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 102598 MW; F898CAAB0256704A CRC64;
MNHLSVSESA NAALIEEYHQ RWLDDANSVD PTWRAFFQGF TLAGGHLTPT AAAKVGEVNI
VDSLKQAHVH YLINAYRALG HTQAHLDPLS GPPAPQPRLQ LAQFNLTEAD LDTVFDTGTY
LGGAQMKLSD IIATLQQTYC GHIGVEYAHI QDTDARRWLQ ERIESTRLQP KFTKPQKVRI
LRRVHKAELF EKFLHTKYVG QKRFSLEGGE TIIAALDAVI DHCPGAGVEE IVMGMAHRGR
LNVLCSVMRK SFDLLFEQFS ENYIPDTVAG DGDVKYHLGY ESILTTTSGK KVEVRLAANP
SHLEIVNPVV EGKARARQRI RGDAKERRKV MPLLIHGDAA VAGQGIVAET LNFSQLPGYR
TGGTVHFIIN NQIGFTTDPR DSRSTHYCTD IAKLVEAPIF HVNGDDPEAV CLVAQLAVDF
RVQFKRDVFV DMYCYRKHGH NETDEPSFTQ PMLYRKIAAH KQVSALYTRS LVAADALSEA
EGEAIKAEYS AALEENLAKA RARESAKSEK RRTTTASGAP TDAFKGSNAI FQPVFKHTPV
ATAVPAATLD RVVQALTTVP AGFKIHSKIK RFIEGRAEAH QNGGPYDWGM GEALAFGTLL
LDGTPVRLSG QDCERGTFTH RHAVFNDTES GEKYTPLNHI AEQQGKFCVY NSLLSEAAVL
GFDYGYSLDY PDMLCIWEAQ FGDFVNGAQV VIDQFITSGE SKWQRCSGIT LLLPHGYEGQ
GPEHSSARLE RFLQACAENN IQVANLTTPA QLFHALRRQT MRDFKKPLVI MSPKSLLRHP
AAVSGLEDFT QANFQEIIDD PIDSGKCDRL ILCSGKVYYD LVDYREKNKI PHTAIIRIEQ
LYPLHRDRLG QLADEYGRDA RLIWCQEEPQ NMGAWSFLAP QLEEIFGRKP VYAGRDAASS
PAVGLLALHR AQLANFLNRA FTA
//
