ID Q7DDJ9_NEIMB Unreviewed; 942 AA.
AC Q7DDJ9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:AAF41361.1};
GN OrderedLocusNames=NMB0955 {ECO:0000313|EMBL:AAF41361.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41361.1, ECO:0000313|Proteomes:UP000000425};
RN [1] {ECO:0000313|EMBL:AAF41361.1, ECO:0000313|Proteomes:UP000000425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 {ECO:0000313|EMBL:AAF41361.1,
RC ECO:0000313|Proteomes:UP000000425};
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF41361.1; -; Genomic_DNA.
DR PIR; C81139; C81139.
DR RefSeq; NP_273993.1; NC_003112.2.
DR RefSeq; WP_002213758.1; NC_003112.2.
DR AlphaFoldDB; Q7DDJ9; -.
DR STRING; 122586.NMB0955; -.
DR PaxDb; 122586-NMB0955; -.
DR KEGG; nme:NMB0955; -.
DR PATRIC; fig|122586.8.peg.1210; -.
DR HOGENOM; CLU_004709_1_0_4; -.
DR InParanoid; Q7DDJ9; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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:AAF41361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000425};
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; 105082 MW; 03322FE321984D4F 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 QAEADGYIQA YRDALDKGEH VEQTTLSNFQ RTQIDWSKYQ
GKDWREHIET GLPAADIERL TEKFTAVPEG FALHPTAKRV IEARKAMASG KQAIDWGMAE
TLAYASLVTK GHGVRISGED SGRGTFSHRH AVLHDQKREK 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 AL
//
