ID   C6SJH6_NEIME            Unreviewed;       942 AA.
AC   C6SJH6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:CBA07147.1};
GN   ORFNames=NMW_1096 {ECO:0000313|EMBL:CBA07147.1};
OS   Neisseria meningitidis alpha275.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=295996 {ECO:0000313|EMBL:CBA07147.1};
RN   [1] {ECO:0000313|EMBL:CBA07147.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Alpha275 {ECO:0000313|EMBL:CBA07147.1};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(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; AM889138; CBA07147.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6SJH6; -.
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:CBA07147.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..791
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   942 AA;  105080 MW;  6B572AA512EB2D25 CRC64;
     MMDEKLNFSY LFGSNAPYIE ELYEAFLENP DAVDEKWKQY FTDLSKQPGT VAVDVAHTPI
     RESFVTLAKK KIASAVAGGA DEAMLKKQVS VLRLISAYRI QGVGAAQLDP LKRIPPRDIE
     ALDPKFHGLS DADMALQFNM GEGDFANRGK LPLSQIISNL KQTYCGHIAL EYIYIPNTEE
     RRWVRNYFES VLSTPHYNAD QKRRILKEMT AAETLERYLH TKYVGQKRFG VEGGESAIAG
     LNYLIQNAGK DGVEEVIIGM AHRGRLNVLV NILGKKPGDL FAEFEGRAEI KLPSGDVKYH
     MGFSSDIATP HGPMHVSLAF NPSHLEIVNP VVEGSARAKQ KRLGENGRDK VLPVLIHGDS
     AFIGLGVNQA TFNLSKTRGY TTGGTVHIVI NNQIGFTTSD IRDTRSTVHC TDIAKMVSAP
     VIHVNGDDPE RVCFAIQAAL DYRKKFHKDI VIDVVCYRKW GHNEGDDPTL TQPMMYKKVS
     QHPGARALYT EQLIAEGVVT QAEADAYIQA YRDALDKGEH VEQTTLSNFQ RTQIDWGKYQ
     GKDWREHIET GLPAADIERL TEKFTAVPEG FALHPTAKRV IEARKAMASG KQAIDWGMAE
     TLAYASLVTK GHGVRISGED SGRGTFSHRH AVLHDQNREK WDDGTYVPLR HMGEGMGEFL
     VIDSILNEEA VMAFEYGFAC SAPDKLTIWE AQFGDFANGA QVTIDQFLSS GETKWGRLCG
     LTTILPHGYD GQGPEHSSAR VERWLQLCSE NNMQVIMPSE ASQMFHLLQR QVLGSYRKPL
     VIFMSKRLLR FKGAMSPLEN FTEGSTFRPV IGDTAERASN DSVKRVVLCA GQVYYDLEAG
     RAERKLEDDV AIVRVEQLYP FPYDEVKAEL AKYPNAKSVV WAQEEPKNQG AFYQIRHRIE
     DVISEEQKLS YAGRPSSASP AVGYSSKHIA QLKQLVEDAL VL
//