ID J9YZE1_9PROT Unreviewed; 950 AA.
AC J9YZE1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=HIMB59_00002640 {ECO:0000313|EMBL:AFS48467.1};
OS alpha proteobacterium HIMB59.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS48467.1, ECO:0000313|Proteomes:UP000006097};
RN [1] {ECO:0000313|EMBL:AFS48467.1, ECO:0000313|Proteomes:UP000006097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB59 {ECO:0000313|EMBL:AFS48467.1,
RC ECO:0000313|Proteomes:UP000006097};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (AUG-2012) 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; CP003801; AFS48467.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YZE1; -.
DR STRING; 744985.HIMB59_00002640; -.
DR KEGG; apc:HIMB59_00002640; -.
DR PATRIC; fig|744985.3.peg.264; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000006097; 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:AFS48467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006097};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 586..779
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 950 AA; 108125 MW; 1337C4F80B2634B6 CRC64;
MRSYNSFLTA NNASQIISIY KDFVKNPSSV DQSWHNFFKE LAPEELAILA DYEKLDWSKK
ARSSDFSQTS LNQAISDSLR LVMMIRAYRE IGHLIANLDP LNLAVQSKPA GLDPEYYGFQ
EKDLDRKIFL FGYLGFETAS VRQVFDKLQK IYSGTLSIEY KHIQSAEEYL WLKDRIEDRK
DMQLTPRGKR TILERLISAE YFEKFLDTKY RGTKRFGLDG AESTIPALEQ ILKRSSEYGI
EDFSFACAHR GRLNILANVV KKPHIQIFSE FIHGGENALS NEGSGDVKYH LGASSDRSFS
GNLIHVSMAA NPSHLEAVNP VVAGKIRAKQ ALVGDKNNEK VSGLLIHGDA AIAGQGVVAE
TFTMSQLNGY RIGGLIHFII NNQIGFTTAP QYSRSAPYSS EIGKIVQAPI FHVNGDDPEA
VVLASRAATE FRNSFKKDTL VDMFCYRKHG HNEGDEPSFT QPLMYQTIKK KKPVAEIYAQ
KLIEQEVLNS KQVEYIKDAV WSDLEKKFEK AKNYKLKTKS WMGGQWSGLS RAPKDTLRRG
RTAEPTKSLQ DIGKKITQVP KDFNLHPKLE KFNSSRLKAI QSGKNIDWAF AEALAFGSLL
KEGFKVRLAG QDSGRGTFSQ RHSVFYDQKT EERYIPLNHI AKKQKQFEVI DSFLSEMGVL
GFEYGYSLAD PNSLVIWEAQ FGDFANGAQI IIDQFIAASE RKWMQMSGLV MLLPHGHEGM
GPEHSSARIE RFLQMAAEDN IQILNCTTPA SYFHALRRQI HRNFRKPLII FTPKSTLRHP
NNVSNIEDFT GRSAFHRIID EDIKNPKRVV FCSGKIFYEL DDYRKENKIK DVKIVRLEQI
YPFPFDTLGE VILKHKDAEM LWVQEEPKNM GAWAFVKSRI RHLFKKHDLE KNLHYVGRRR
AAAPATGIAK RHNANQNLIK KLALHSPLKS VIKEKIGVSF IKFKNLPTNE
//
