ID F9GQH5_HAEHA Unreviewed; 935 AA.
AC F9GQH5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:EGT74569.1};
GN ORFNames=GG9_1500 {ECO:0000313|EMBL:EGT74569.1};
OS Haemophilus haemolyticus M19501.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1028803 {ECO:0000313|EMBL:EGT74569.1, ECO:0000313|Proteomes:UP000003258};
RN [1] {ECO:0000313|EMBL:EGT74569.1, ECO:0000313|Proteomes:UP000003258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M19501 {ECO:0000313|EMBL:EGT74569.1,
RC ECO:0000313|Proteomes:UP000003258};
RX PubMed=21952546; DOI=10.1128/JB.05863-11;
RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D.,
RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J.,
RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A.,
RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., Rowe L.,
RA Frace M., Mayer L.W.;
RT "Genome Sequences for Five Strains of the Emerging Pathogen Haemophilus
RT haemolyticus.";
RL J. Bacteriol. 193:5879-5880(2011).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGT74569.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQO01000015; EGT74569.1; -; Genomic_DNA.
DR RefSeq; WP_005632547.1; NZ_AFQO01000015.1.
DR AlphaFoldDB; F9GQH5; -.
DR PATRIC; fig|1028803.3.peg.1567; -.
DR eggNOG; COG0567; Bacteria.
DR Proteomes; UP000003258; Unassembled WGS sequence.
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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 106495 MW; 44E33F2CEBE8ED00 CRC64;
MQQNKAFDDW LASTALGGAN QSYIEELYES YLSDPQSVEE SWRATFDSLP KTTALEQPHT
PVRDYFRRLA RENHNEAVTV IDPAAGAKLV KVLQFINAYR FRGHLEANLD PLNYYRWKVS
SVPELDYRHH GFTEQDLNET FNINHYVYKR DTIKLGELAQ MLKETYCGSI GLEFMHVQDM
AQKTWLQSKM ESVLDKPLFT SEERVNFLRE LTAADGLERY LGAKFPGAKR FSLEGSDAFI
PLMKEIIRHA SRQGVNNVVM GMAHRGRLNM LVNVLGKKPE NLFDEFAGKH SSERTGDVKY
HQGFSSDFAV DDKRVHLTLA FNPSHLEIVS PVVIGSVRSR QTRMNDTEHS KVLAITVHGD
SAVAGQGVVQ ETLNMSNSRG YSVGGTIRIV INNQIGFTTS NPNDTRSTEY CTDIAKMIQA
PIIHVNGDDP EAVAFAARMA VEYRNLFKRD IFIDLISYRR HGHNEADEPL ATQPMMYSII
KKHPTPRKVY ADRLVSEGVM TEEQVTEMVN DYRDALDNGD RVVSEWREMD TAKMDWLQYL
NYDWTAPYES KFSQERFLTL AKRVCEYPES LRAHPRVEKI YNDRKAMYQG EKLLDWGMAE
TMAYATLLDE GVNVRLSGED AGRGTFFHRH AVVHNQNDGT GYVPLTHLHA NQGRFEVWDS
VLSEESVLAF EYGYATTDPK TLTIWEAQFG DFANGAQIVI DQFISSGEQK WGRMCGLVML
LPHGYEGQGP EHSSARLERY LQLCAEQNMQ VCVPSTPAQV YHMLRRQSLR KMRRPLIAIS
PKSLLRHPLA VSSLDELING AFQTVIGEID ELDPKDVKRV VMCSGKVYYD LLEQRRANNQ
KDVAIIRIEQ LYPFPHEDVK KALESYAHVS DYVWCQEEPL NQGAWYCSKH NFESAIPESV
KLKYAGRPAS ASPAVGYMSL HTKQQKQLVE DALSL
//
