ID A0A402D3R6_9BACT Unreviewed; 939 AA.
AC A0A402D3R6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=CCAX7_38990 {ECO:0000313|EMBL:BDI31848.1}, CCAX7_53330
GN {ECO:0000313|EMBL:GCE56819.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE56819.1};
RN [1] {ECO:0000313|EMBL:GCE56819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE56819.1};
RA Li J., Tonouchi A.;
RT "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:BDI31848.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31848.1,
RC ECO:0000313|Proteomes:UP000287394};
RA Li J., Kudo C., Tonouchi A.;
RT "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT class Armatimonadia of the phylum Armatimonadetes.";
RL Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN [3] {ECO:0000313|EMBL:BDI31848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31848.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) 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; AP025739; BDI31848.1; -; Genomic_DNA.
DR EMBL; BHFQ01000018; GCE56819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402D3R6; -.
DR KEGG; ccot:CCAX7_38990; -.
DR InParanoid; A0A402D3R6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000287394; 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:UP000287394};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 581..776
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 505..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 102335 MW; 2E481A1DA89F3620 CRC64;
MSELSRFFGP NAGYVLDLYD QYQENPESVD PETRAFFADW SPPAGLGSPP VSEGGVVAAI
DVNKIVATAR VARLVRELGH LTAHIDPLGS PPPGDPGLEL ETHGLQTRDL TTLPASVVGG
PLAVGAPNAL EALGRLRRVY SGTIGYEDDH IQVDEERKWI VDAIETRRFF QDFDATQKID
VLKRLTEVET FERFLHTTFI GAKRFSIEGT DMVVPILDAI IHAASVADTR EIVMGMAHRG
RLNVLAHILG KPYSAILAEF QAAKDESSAV SGTGSSGWTG DVKYHMGARR NYSENGGHEM
PITLAPNPSH LEFVDPVAVG RARAAQETRQ GRRKTLHDPS ASLAILIHGD AAFPGQGVVA
ETLNLSQLFG YDVGGTIHII TNNQIGFTTS PRDSRSTLYA SDLAKGFEIP IVHVNADDPE
ACIAAARMAH AYRERFGKDF LIDLVGYRRW GHNEGDEPSF TQPRMYENIS THPTVRELWG
RELERAGLLT RDEVNAMIKT VQDTLQEART TPSGRGLSKG PLPYGSGENS LPHVDTAVPA
ERLIELNEAL LARPVGFTAN AKLDRTLIVR RRAGIQEENG IEWAHAEALA FASILTEGTP
IRLSGQDAER GTFSTRHSVL HDPTTGERYT PLQELPQSTA SFAVYNSPLS ETAALGFEYG
YSMHAAGVLV LWEAQFGDFV NGAQVIVDQF LVSGNAKWLQ TPSLVLLLPH GYEGQGPEHS
SGRVERFLQL AASDNIRIVN CTTAAQYFHV LRRQAALLHT APRPLIIMTP KGLLRHPKAA
SSLQDLATGH FQTVIDDAAA RSHASDISRI VLSSGKVYVD LIGNEAFAEA SSHLAAVRVE
QLYPFPGDVL RDTLASYPNA QEIVWMQEEP KNMGAWTYME PKLRDLLAPG QTLTYVGRPE
SASPAEGSIR RHTTEQNRIV AAALSAAPAL KVKKAVVKS
//
