ODO1_HAEIN
ID ODO1_HAEIN Reviewed; 935 AA.
AC P45303;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN Name=sucA; OrderedLocusNames=HI_1662;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000250|UniProtKB:P0AFG3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000250|UniProtKB:P0AFG3}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23308.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23308.1; ALT_INIT; Genomic_DNA.
DR PIR; E64135; E64135.
DR RefSeq; NP_439804.2; NC_000907.1.
DR RefSeq; WP_010869267.1; NC_000907.1.
DR AlphaFoldDB; P45303; -.
DR SMR; P45303; -.
DR STRING; 71421.HI_1662; -.
DR PRIDE; P45303; -.
DR EnsemblBacteria; AAC23308; AAC23308; HI_1662.
DR KEGG; hin:HI_1662; -.
DR PATRIC; fig|71421.8.peg.1740; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR PhylomeDB; P45303; -.
DR BioCyc; HINF71421:G1GJ1-1679-MON; -.
DR Proteomes; UP000000579; 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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.11610; -; 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 PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 3: Inferred from homology;
KW Glycolysis; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..935
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000162194"
SQ SEQUENCE 935 AA; 106806 MW; 33607F3C3AFDDC78 CRC64;
MQQNKAFDDW LASTALGGAN QSYIEELYES YLSDPQSVEE SWRKTFDSLP KTTALEQPHT
PVRDYFRRLA RENHNEAVTV IDPAAGAKLV KVLQFINAYR FRGHLEANLD PLNYYRWKVS
FVPELDYRHH GFTEQDLNET FNINHYVYKR DTIKLGELAQ MLKETYCGSI GLEFMHVQDM
EQKMWLQSKM ESLLDKPLFT SEERVNFLRE LTAADGLERY LGAKFPGAKR FSLEGSDAFI
PLMKEIIRHS SRQGVNDVVM GMAHRGRLNM LVNVLGKKPE NLFDEFAGKH SSERTGDVKY
HQGFSSDFAV DDKRVHLTLA FNPSHLEIVS PVVIGSVRSR QTRMNDTEHS KVLAITVHGD
SAVAGQGVVQ ETLNMSNTRG YSVGGTIRIV INNQIGFTTS NPNDTRSTEY CTDIAKMIQA
PIIHVNGDDP EAVAFAARMA VEYRNLFKRD IFIDLISYRR HGHNEADEPL ATQPMMYSII
KKHPTPRKVY ADRLVSEGVM TEEQVTEMAN 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 TFQTVIGEID ELDPKDVKRV VMCSGKVYYD LLEQRRANNQ
KDVAIIRIEQ LYPFPHEDVK KALEPYAHVT DYVWCQEEPL NQGAWYCSKH NFESAIPESV
KLKYAGRPAS ASPAVGYMSL HTKQQKQLVE DALSF
