ID   B4ESQ9_PROMH            Unreviewed;       934 AA.
AC   B4ESQ9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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:CAR41366.1};
GN   OrderedLocusNames=PMI0569 {ECO:0000313|EMBL:CAR41366.1};
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR41366.1, ECO:0000313|Proteomes:UP000008319};
RN   [1] {ECO:0000313|EMBL:CAR41366.1, ECO:0000313|Proteomes:UP000008319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320 {ECO:0000313|EMBL:CAR41366.1,
RC   ECO:0000313|Proteomes:UP000008319};
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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; AM942759; CAR41366.1; -; Genomic_DNA.
DR   RefSeq; WP_004244418.1; NC_010554.1.
DR   AlphaFoldDB; B4ESQ9; -.
DR   EnsemblBacteria; CAR41366; CAR41366; PMI0569.
DR   GeneID; 6800883; -.
DR   KEGG; pmr:PMI0569; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000008319; 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:CAR41366.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          592..785
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   934 AA;  105458 MW;  FB2F359606B9754E CRC64;
     MQNGAMKDWL DSTFLAGENQ SYIEEIYEDY LTDPNSVDES WREIFQQLPV SQGAEQSHSQ
     TRDYFRRLAK ESTRYHTSVS DPAMDSKQVK VLQLINAFRF RGHQNANLDP LGLWKRESVP
     DLDPAFHNLT KEDFEETFNV GSFAIGKETM KLGDIYEALK RIYCGSIGAE YMHITNTEEK
     RWIQQRLESV NVADQFTKEE KIRFLAELTA AEGLERYLGA KFPGAKRFSL EGGDALIPML
     KDLIRHAGKQ DTREVVLGMA HRGRLNVLVN ILGKKPADLF DEFAGIHKEH LGTGDVKYHQ
     GFSSDFATEG AQVHLALAFN PSHLEIVSPV VIGSVRARRD RLDEARSNMV LPITIHGDAA
     VTGQGVVQET LNMSQARGYE VGGTVRIVIN NQVGFTTSNP KDARSTEYCT DIVKMVQAPI
     FHVNADDPEA VAFVTRLALD FRNTFKRDVM IDLVCYRRHG HNEADEPNAT QPLMYQKIKK
     HPTPRKIYAD KLVEQGLIEA NDVTELVNLY RDALDRGDCV VEEYRPMGLH SYTWEPYLNH
     EWNEEYPHKV EKSRLQDLAR RVSTVPSEIA MQSRVEKIYA DRAVMAEGEK LLDWGAAETL
     AYATLVDQGI TIRLSGEDAG RGTFFHRHAV IHNQTNGSVY VPLANIHNAQ GQFNVWDSVL
     TEEAVLAFEY GYATTEPRGL TIWEAQFGDF ANVAQVVIDQ FISSGEQKWG RMCGLVMLLP
     HGYEGQGPEH SSARLERYLQ LCAEQNMQVC VPSTPAQVYH MLRRQALRGM RRPLIVMSPK
     SLLRHPLAVS SLDELADGKF LPVIGELDEL NPADVKRVVM CSGKVYYDLL EQRRANGQTD
     VAIIRIEQLY PFPHDDMAQI LAPYAHVKDF IWCQEEPLNQ GAWYCSQHNF RDAIPTGATL
     RYAGRPASAS PAVGYTSVHQ EQQKALVEDA LKVE
//