ID A7HT41_PARL1 Unreviewed; 1083 AA.
AC A7HT41;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=Plav_1454 {ECO:0000313|EMBL:ABS63074.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS63074.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS63074.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(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 -!- 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; CP000774; ABS63074.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HT41; -.
DR STRING; 402881.Plav_1454; -.
DR KEGG; pla:Plav_1454; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR Proteomes; UP000006377; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; cd00093; HTH_XRE; 1.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_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; PF13560; HTH_31; 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; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 728..921
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 87..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 121224 MW; A08E676124D4206B CRC64;
MPSRQNALTG PLPLWQFSSM KLSDWLETNN LTASAFAEQL GVSVSTVTRC MNGQRRPEWP
TLDSIFKATG GAVTPNDFLS DAAALQGTAP ASPKPNGSDP MSSNGSNDRF ERTSFLYGGN
ALFVEQLYAR YQKDPQSVDA EWRTFFESLG DAPEDVLKEA RGASWQRADW PIAANGELVS
ALDGNWGATT AVEAGKVKDK IAERRPAASE EEIRAATLDS VRALMMIRAY RIRGHLDADI
DPLKLRPKSQ HPELQPESYG FGPDDLDRPI FIDHVLGLET ATVREMLDIL RRTYCGTLAV
EFMHIGDPEE KAWIQERIEG PDKEIAFTDM GRSAILDKLI QAEGFEKFCG VKYVGTKRFG
LDGAEAMIPA LEQIIKRGGA LGAKEIVFGM AHRGRLNVLT NVMSKPYHAV FHEFKGGSST
PEDVDGSGDV KYHLGASSDR EFDGNKVHLS LTANPSHLEI VDPVVLGKAR AKQDQHHDRQ
RGSVIPLLIH GDAAFAGQGI VAECLGLSDL KGHRTGGSIH FIINNQIGFT TSPINSRSSP
YPSDVAKMVQ APIFHVNGDD PEAVVHAAKI ATEFRQRFNK PVVIDMFCYR RFGHNEGDDP
SMTQPLMYEK IKDHPTTLQI YSQRLIEENL MTAAEVDERL AAFRAELESH YEAAGTFRPN
KADWLDGRWS GFSKAEGEAR RGETAVEVDR LREIGRKITE VPEGFHIHKT IQRFLDNRRK
SIETGEGIDW STAEALAFGS LVSEGIKVRL SGQDSERGTF VQRHSVLNDQ QTEDRYVPLN
NISEGQAEYE VINSMLSEAA VLGFEYGYSL AEPNALVLWE AQFGDFANGA QVVIDQFISS
GERKWLRMSG LVMLLPHGYE GQGPEHSSAR LERFLQMCAE DNMQVANCTT PMNYFHILRR
QMHRKFRKPL ILMTPKSLLR HKRAVSRIEE FGAGSSFHRV LWDDAELLPD QKIKLLPDKD
IKRVVLCSGK VYYDLYEERE RRGINDIYIL RVEQLYPVPA KSLMTELARF PEAEFVWCQE
EPKNMGAWNF IEPNIEWVLN HVGTRYRRAT YAGRPASAAT ASGLMSRHNQ ELNQLLSEAL
KID
//
