ID A0A0C5WK40_9FLAO Unreviewed; 913 AA.
AC A0A0C5WK40;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=AW14_05140 {ECO:0000313|EMBL:AJR03115.1};
OS Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Siansivirga.
OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR03115.1, ECO:0000313|Proteomes:UP000032229};
RN [1] {ECO:0000313|EMBL:AJR03115.1, ECO:0000313|Proteomes:UP000032229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR03115.1,
RC ECO:0000313|Proteomes:UP000032229};
RA Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL Submitted (FEB-2014) 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; CP007202; AJR03115.1; -; Genomic_DNA.
DR RefSeq; WP_044637818.1; NZ_CP007202.1.
DR AlphaFoldDB; A0A0C5WK40; -.
DR STRING; 1454006.AW14_05140; -.
DR KEGG; sze:AW14_05140; -.
DR PATRIC; fig|1454006.5.peg.1008; -.
DR HOGENOM; CLU_004709_1_0_10; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000032229; 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:UP000032229};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 578..771
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 913 AA; 104002 MW; C2B36D806C717559 CRC64;
MDKFSFLNAA HTAYFADLYD QYLQNPDSVE PSWRAFFQGY DFGSENYGFE GEIVEGVSAQ
MPEYLQKEFQ VIKLIDGYRM RGHLFTKTNP VRDRRTYEPT LDIENFGLSA NDLDTVFNAG
EILGIGAKPL REILVHLNKI YCSSIGVEYM YLRNPEVISW WQGKLNHNDN QPSFSATKKK
YILSKLNQAV TFENFLQTKY VGQKRFSLEG GESLIPAISN VLFVAAEKYD VKECVLGMAH
RGRLSTLVNI FRKPVNELFS EFDGKDFEDA DIDGDVKYHL GLTLDKTYQN GKNIKMNLVP
NPSHLETVAS VAEGITRAKI DTDYNGDDQK IIPIIVHGDA AIAGQGIVYE VAQMSQLNGY
KTGGTVHIVV NNQIGFTTNY LDARSSTYCT DVAKVTLSPV LHVNADDAEA VVHAVELALE
YRMRYKKDVY IDLLGYRKYG HNEGDEPRFT QPKLYKAIAK HKNPFEIYSS KLISEKTIDK
DYVDAIVEEF KSTLEAEYIK SKEADSSKVR EFMQERWQGF EREDLEGMLK PVDTSYPKEN
LENISKVVST VPKDVKFVRK AERILEGRAK MVFETDTLDW GMAETLAYGS LLEEGFNVRI
SGQDVERGTF SHRHAILRDE ISEERVNLLN LNPHNKGKMD IFNSFLSEYG VLGFDYGYAM
ANPNTLTIWE AQFGDFSNGA QIIFDQYLSA AEDKWKSQNG IVVLLPHGYE GQGSEHSSAR
IERYLQLCGD DNMTVADCTT PANMYHLLRR QMLRKFRKPL IVFTPKSLLR HPKAVSSISE
LASGEFQEVI DDTINPENVK KLVLCTGKFY YDLLAEREEL GREDIALVRI EQLFPLHIDK
IQAAINRYPN VEKYVWAQEE PRNMGAWSYL TQRLDIVKLE GITRPYNSVP APGSGTRDKS
RQRRVINAVF ENN
//