ID   A3MZH3_ACTP2            Unreviewed;       936 AA.
AC   A3MZH3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
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:ABN73559.1};
GN   OrderedLocusNames=APL_0455 {ECO:0000313|EMBL:ABN73559.1};
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN73559.1, ECO:0000313|Proteomes:UP000001432};
RN   [1] {ECO:0000313|EMBL:ABN73559.1, ECO:0000313|Proteomes:UP000001432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20 {ECO:0000313|EMBL:ABN73559.1,
RC   ECO:0000313|Proteomes:UP000001432};
RX   PubMed=18065534; DOI=10.1128/JB.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000569; ABN73559.1; -; Genomic_DNA.
DR   RefSeq; WP_009875173.1; NC_009053.1.
DR   AlphaFoldDB; A3MZH3; -.
DR   STRING; 416269.APL_0455; -.
DR   EnsemblBacteria; ABN73559; ABN73559; APL_0455.
DR   KEGG; apl:APL_0455; -.
DR   PATRIC; fig|416269.6.peg.471; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000001432; 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:ABN73559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..787
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   936 AA;  106778 MW;  E0A3EF37CF98BBD5 CRC64;
     MQHKNFEDWL ASSPFGGSNQ TYVEEIYEQY LENPANVDAS WRVIFDTLPK TQVVEQPHSQ
     VRDYFRKLAR ENVPESVTVI DPEASAKQVR LLQWINAHRF RGYLEAKLDP INYYRWKISV
     VPELDYRHHG FTEADLNETV TIGKYVYGKE TMKFGELADA LKQTYLGTIG LEFMHVQDME
     QRNWLQAKIE STLNKPLFTH TEKVNLLTEL TAADGLERYL GAKFPGAKRF SLEGSDAFIP
     MMKEIIRHAG RQGMKDVVMG MAHRGRLNML VNVLGKRPAE LFDEFAGKHA DDNRTGDVKY
     HQGFSSDFDV DGERVHLTLA FNPSHLEIVS PVVIGSVRAR QERIRDTEHN KVLAVTVHGD
     SAVAGQGVVQ ETLNMSNARG YKVGGTIRIV INNQIGFTTS NPNDTRSTEF CTDIAKMIQA
     PIIHVNGDDP EAVAFAARMA VEYRTLFKRD IFIDLISYRR HGHNEADEPL ATQPMMYSII
     KKHPTPRKVY ADRLVAEGVL NQDQATEIMN NYRDALDNGD RVVPEWREMD MAAVDWLQYL
     NYDWTAPYES KFPQDRFYTL AKRVCEYPES LRPHSRVEKI YSDRKEMYEG KKLLDWGMAE
     TMAYATLLDE GTHVRLSGED AGRGTFFHRH AVVHNQNDGT GYVPLAHLHA NQGRFEVWDS
     VLSEEAVLAF EYGYATTDPK TLTIWEAQFG DFANGAQIVI DQFISSGEQK WGRMCGLVML
     LPHGYEGQGP EHSSARLERY LQLCAQQNMQ VCVPSTPAQA YHMLRRQAIR KMRRPLVAIT
     PKSLLRHPLA VSSLEELTEG EFQNVIGEID SNIAAKKVKR VVMCSGKVYY DLLEQRRQNE
     QTDIAIIRIE QLYPFPYEDM KKVLEPYAHV KDFVWCQEEP QNQGAWYCSK HNFEASIPEK
     AKLTYAGRPA SASPAVGYTS LHAQQQKQLV DDALTL
//