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Database: UniProt
Entry: A0A023D2S6_ACIMT
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ID   A0A023D2S6_ACIMT        Unreviewed;       963 AA.
AC   A0A023D2S6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=Amme_023_035 {ECO:0000313|EMBL:GAJ28442.1};
OS   Acidomonas methanolica NBRC 104435.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidomonas.
OX   NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ28442.1, ECO:0000313|Proteomes:UP000019760};
RN   [1] {ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX   PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
RN   [2] {ECO:0000313|EMBL:GAJ28442.1, ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|EMBL:GAJ28442.1,
RC   ECO:0000313|Proteomes:UP000019760};
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
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}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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:GAJ28442.1}.
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DR   EMBL; BAND01000023; GAJ28442.1; -; Genomic_DNA.
DR   RefSeq; WP_042057035.1; NZ_BJVB01000012.1.
DR   AlphaFoldDB; A0A023D2S6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000019760; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019760};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          616..809
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   963 AA;  104807 MW;  575332BF6B3089A5 CRC64;
     MGEIGFSSML NGANTVYLAD LQARWAQDPN SVDPSFAQFF ATLDDESARI LADASGASWA
     PHHSFIEGIE GGTSVNEAER MAPMAPATPA GLAGSIDDSL RAVQLMRAYR VRGHLEARLD
     PLGLKIPAPH ADLDPATYGF GEDDRERPIY LGRVLHALMP DRDAATIHEL VAALRATYCG
     SIGAEFMHIQ AADQRAWIQK RLEGDNWQAG LPADARKVVL TQLTEAEGFE SFCQKRYTGT
     KRFGLEGSEI TIPVLHAIID QSVRSGTASV SLGMAHRGRL NTMANIVQKP FAAIFSEFAG
     ASFKPGDVQG SGDVKYHLGT AATLRVAGHD VRVSLLPNPS HLEAVDPVVV GRVRALQDRD
     GSVGKAERHR HLGVLVHGDA AFAGQGIVYE TMAMSQLIGY RTGGTVHVVT NNQIGFTTVS
     AHAYSGMYCT DIAKAVQAPI LHVNGDDPDA AVYAARLSAD FRREFATDIV LDLVGYRRHG
     HNEADEPAFT QPVMYQAIAA RPTLRTLYAQ KLAEEGVMDK ALSDAQWQDF QDHLQAEFEV
     AKGYKPNLAD WMDTGQDPSQ IAQGRKAGEP LTGIGETALE EIGRAMTQVP KDFTLHPRLK
     RVIQARADAI EGGDGIDWAT GEALAFGSLM LEGHRVRLSG EDCQRGTFSQ RHAVLIDQKT
     QTEYTPLNAM PNARAKLEVY NSLLSEFGVL GFEYGYSLTD PATLVLWEAQ FGDFANGAQV
     IIDQFIASGE TKWLRTSALV MLLPHGFEGQ GPEHSSARLE RYLQLCAEDN MRVGNITTPA
     NYFHALRRQL FPGSRKPLVL MTPKSLLRNK AAVSKLADFL PGTAFQPVLA ETDELAPDVE
     ISRVVLCSGK VYYDLHAARQ EAGRRDIAIL RLEQFYPFPQ ADLAAALARY PNATVIWCQE
     EPENSGAWSF VDRRIEKTLT AVGHKAGRPS YVGRPEGASP ATGLASEHVA QQQQLIAEAL
     GLA
//
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