ID F0SE02_PSESL Unreviewed; 926 AA.
AC F0SE02;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Pedsa_2380 {ECO:0000313|EMBL:ADY52928.1};
OS Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG
OS 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pseudopedobacter.
OX NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY52928.1, ECO:0000313|Proteomes:UP000000310};
RN [1] {ECO:0000313|EMBL:ADY52928.1, ECO:0000313|Proteomes:UP000000310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RX PubMed=22180808; DOI=10.4056/sigs.2154937;
RA Liolios K., Sikorski J., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kotsyurbenko O., Rohde M., Tindall B.J., Abt B., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of the gliding, heparinolytic Pedobacter saltans
RT type strain (113).";
RL Stand. Genomic Sci. 5:30-40(2011).
RN [2] {ECO:0000313|Proteomes:UP000000310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 /
RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Pedobacter saltans DSM 12145.";
RL Submitted (FEB-2011) 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; CP002545; ADY52928.1; -; Genomic_DNA.
DR RefSeq; WP_013633414.1; NC_015177.1.
DR AlphaFoldDB; F0SE02; -.
DR STRING; 762903.Pedsa_2380; -.
DR KEGG; psn:Pedsa_2380; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_10; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000000310; 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:ADY52928.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000310};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 576..769
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 926 AA; 105727 MW; FC2355A5AA6F3434 CRC64;
MDNLSYLSNA DSAYIDSLYQ SYKENPQSVD FGWQKFFEGF DFGLQSDADG SVPQPVISGA
TPDHVLKEIN VLNMIDGFRT RGHLFTKTNP VRERRKYYPG KELETFGLSD ADLDTVFNAG
VEIGLGPAKL RDIYQLLNET YCESIGVEYK YMRNPLKFKW FEERIELSRN KPQFDIEKKK
RILQKLNQAV VFESFLGTKF LGQKRFSLEG AEALIPALDS VIEKGAELGI EEFTIGMAHR
GRLNVLTNIM GKTYKDVFSE FEGKYNKDLP FGGDVKYHLG FSTDVETSSN KKVHLSLCPN
PSHLETVAAV VEGITRSKID MKYGRDYNRI APIVIHGDAS VAGQGLVYEV LQMSKLDAYK
TGGTIHLVIN NQIGFTTNYK DARSSTYCTD IAKVTLSPVF HVNGDDVEAL VYAINMAVEY
RQRFHNDVFI DILCYRRYGH NESDEPRFTQ PLLYKKIEKH PNPREIYVDK LKAQGAVDAN
LAKQMDKEFR ELLQERLNES KEDPGAPENP TYSGAWSDLR ISTAKDLVNS PDTSVDEKTF
VQIANKITTL PSDKKFLSKV DRLFSDRKKM IENKSFDWAM GELMAYGTLV NEGRRVRISG
QDVERGTFSH RHAVIRVEES EEQYTPLHHV REGQGPFEIY NSHLSEYGVL GFEYGYAMAN
PYSLTIWEAQ FGDFANGAQI VIDQYISSAE TKWQRGNGLV MLLPHGYEGQ GPEHSSARIE
RFLELCAEDN MQIVYCSTPA QLFHALRRQL KRDFRKPLVN FSPKSLLRNP KCVSSLDDFT
KGKFREVIDD VNVTAKDVKR VAICSGKIYY DLLEEQEKNN RKDVALVRLE QIYPTPFEQL
NAIREKYKNA EFYWVQEEPE NNGPWPFICR VFRKSNFDFE VISRRASSSP ATGFAKQHVA
EQNEIISKVF NLEGDKITDS KKAKTK
//
