ID   A1AZH3_PARDP            Unreviewed;       988 AA.
AC   A1AZH3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   OrderedLocusNames=Pden_0555 {ECO:0000313|EMBL:ABL68667.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68667.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP000489; ABL68667.1; -; Genomic_DNA.
DR   RefSeq; WP_011746900.1; NC_008686.1.
DR   AlphaFoldDB; A1AZH3; -.
DR   STRING; 318586.Pden_0555; -.
DR   EnsemblBacteria; ABL68667; ABL68667; Pden_0555.
DR   GeneID; 75500098; -.
DR   KEGG; pde:Pden_0555; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
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:ABL68667.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          633..826
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   988 AA;  110035 MW;  AFD02BC822FD0FE5 CRC64;
     MNDQSPNSAF HDSSFLQGHN AAYVEQLYGQ WAQNPAAVDQ AWDAFFRSLG DDEAVVTREA
     KGASWHRADW PPVPADDTTA ALTGEWPMLP KTEAKAALDK IAAKAGEKGV NLTDDQLKRA
     VLDSVRAIML IRAFRIRGHL HADLDPLGMR EIPDHGELDP KTYGFSEADL DRPIFIDNVL
     GLQIATIRQI VDLMSRTYCG TFALQFMHIS NPEEAAWLKE RIEGYGKEIA FTREGRRAIL
     NKLVEAEGFE KFLHVKYMGT KRFGLDGGEA LIPAMEQIIK RGGALGVKDV VIGMPHRGRL
     SVLANVMGKP YRAIFHEFQG GSYKPDDVDG SGDVKYHLGA SSDRTFDDNT VHLSLTANPS
     HLEAVNPVVL GKVRAKQDQL SDHTHRTAVL PILLHGDAAF AGQGIVAECF QLSGIKGHRT
     GGCIHIVVNN QIGFTTAPHF SRTSPYPTDI ALMVEAPIFH VNGDDPEAVV HAARVATEFR
     QKFHKDVVID IFCYRRFGHN EGDEPMFTNP AMYKAIKGHK TTLQRYTERL VADGLVPEGE
     IEEMKAAFQS HLNEEFEVGK NFKPNKADWL DGKWSGIEAE HAEENLGQTG IAPETMAEIG
     SALTRVPEGF DLHRTVGRLL ESKKQMFETG KGFDWATGEA LAFGSLLVEG HPVRLAGQDS
     TRGTFSQRHS AFVDQATEER CYPLNHIRGG QARYEVIDSM LSEYAVLGFE YGYSLAEPNS
     LVMWEAQFGD FANGAQIMFD QFITSGEKKW LRMSGLVMLM PHGYEGQGPE HSSARLERWL
     QMCAEDNWIV ANCTTPANYF HILRRQLKRP FRKPLVLMTP KSLLRHPLAV STADEFLTGS
     TFNRVLVDDA DRGKSEFKLA PDDKIRRVVI CSGKVYYDLA QARDAAGAED VYILRLEQFY
     PFPAQTMSKE LERFKDAEIV WCQEEPKNQG GWTFVEPNIE WVLSRIGAKH GRPRYVGRHA
     AASPATGLAS RHKAEQEALV HEAITIGA
//