ID   Q4QJT1_HAEI8            Unreviewed;       950 AA.
AC   Q4QJT1;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
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:AAX88716.1};
GN   OrderedLocusNames=NTHI1964 {ECO:0000313|EMBL:AAX88716.1};
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX88716.1, ECO:0000313|Proteomes:UP000002525};
RN   [1] {ECO:0000313|EMBL:AAX88716.1, ECO:0000313|Proteomes:UP000002525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP {ECO:0000313|EMBL:AAX88716.1,
RC   ECO:0000313|Proteomes:UP000002525};
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S.Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88716.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4QJT1; -.
DR   KEGG; hit:NTHI1964; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000002525; 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:AAX88716.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          609..802
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   950 AA;  108702 MW;  932B796ACADED75A CRC64;
     MERKYCFKYH NKEVIMQQNK AFDDWLASTA LGGANQSYIE ELYESYLSDP QSVEESWRKT
     FDSLPKTTAL EQPHTPVRDY FRRLARENHN EAVTVIDPAA GAKLVKVLQF INAYRFRGHL
     EANLDPLNYY RWKVSSVPEL DYRHHGFTEQ DLNETFNINH YVYKRDTIKL GELAQMLKET
     YCGSIGLEFM HVQDMEQKMW LQSKMESLLD KPLFTSEERV NFLRELTAAD GLERYLGAKF
     PGAKRFSLEG SDAFIPLMKE IIRHSSRQGV NDVVMGMAHR GRLNMLVNVL GKKPENLFDE
     FAGKHSSERT GDVKYHQGFS SDFAVDDKRV HLTLAFNPSH LEIVSPVVIG SVRSRQTRMN
     DTEHSKVLAI TVHGDSAVAG QGVVQETLNM SNARGYSVGG TIRIVINNQI GFTTSNPNDT
     RSTEYCTDIA KMIQAPIIHV NGDDPEAVAF TARMAVEYRN LFKRDIFIDL ISYRRHGHNE
     ADEPLATQPM MYSIIKKHPT PRKVYADRLV SEGVMTEEQV TEMANDYRDA LDNGDRVVSE
     WREMDTAKMD WLQYLNYDWT APYESKFSQE RFLTLAKRVC EYPESLRAHP RVEKIYNDRK
     AMYQGEKLLD WGMAETMAYA TLLDEGVNVR LSGEDAGRGT FFHRHAVVHN QNDGTGYVPL
     THLHANQGRF EVWDSVLSEE SVLAFEYGYA TTDPKTLTIW EAQFGDFANG AQIVIDQFIS
     SGEQKWGRMC GLVMLLPHGY EGQGPEHSSA RLERYLQLCA EQNMQVCVPS TPAQVYHMLR
     RQSLRKMRRP LIAISPKSLL RHPLAVSSLD ELINGTFQTV IGEIDELDPK DVKRVVMCSG
     KVYYDVLEQR RANNQKDVAI IRIEQLYPFP HEDVKKALEP YAHVTDYVWC QEEPLNQGAW
     YCSKHNFESA IPESVKLKYA GRPASASPAV GYMSLHTKQQ KQLVEDALSF
//