ID A0A2T0VHH3_9MICO Unreviewed; 1273 AA.
AC A0A2T0VHH3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:PRY69523.1};
GN ORFNames=B0I08_102199 {ECO:0000313|EMBL:PRY69523.1};
OS Glaciihabitans tibetensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Glaciihabitans.
OX NCBI_TaxID=1266600 {ECO:0000313|EMBL:PRY69523.1, ECO:0000313|Proteomes:UP000237983};
RN [1] {ECO:0000313|EMBL:PRY69523.1, ECO:0000313|Proteomes:UP000237983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12484 {ECO:0000313|EMBL:PRY69523.1,
RC ECO:0000313|Proteomes:UP000237983};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
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:PRY69523.1}.
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DR EMBL; PVTL01000002; PRY69523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0VHH3; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000237983; Unassembled WGS sequence.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
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; PF00198; 2-oxoacid_dh; 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; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000237983};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 933..1126
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 53..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 139256 MW; 89D1DF5158A0B3FD CRC64;
MSSQVTGVTS EDGTTGEFGA NEWLVDEMYE RYTVDKNSVD RSWWPILESY QPTVKAEEAE
PPPVKDPTPT TSIPIQGQLG GEAQIPAELT SDAAEAGAVA SDSPPSSPSQ PIARTTSVQA
KPQPIPAQAP TAPASKATAA APTDEPNGDE SVVTPLRGMS KSLAANMDAS LSVPTATSVR
TIPAKLMIDN RIVINNHLKR SRGGKVSFTH IIAWAIVETL KEFPSQNVFY DEIDGKPSVV
APAHINLGIA IDLPKPDGTR ALLVPGIKRT DTMDFAEFLV GYEDVVKRAR ANKLTGADFA
GNTISLTNPG GIGTEHSVPR LMRGAGCIVG AGALEYPAAF QGASAKSLAE FGIGKTITLT
STYDHRVIQG AGSGEFLKKI HELLIGERGF YEGIFAALRI PYEPIHWASD ISVDLADAVG
KTARVQELIN SFRVRGHLMA DVDPLEYRQR SHPDLEIESH GLTFWDLDRE FVTGGLGGRK
SALLRDILGT LRDSYCRTIG IEYMHIQDPV QRRWIQGHVE KPYAKPGHND QMRILGKLNE
AEAFETFLQT KYVGQKRFSL EGGECTIALL DALLKDAAED GLDEVAIGMA HRGRLNVLTN
IAGKTYGQIF REFEGTQDPR TVQGSGDVKY HLGTEGTFTN SDGRQLPVYI AANPSHLEAV
DGVLEGIVRA KQDRKPIGTF GVLPVMVHGD AAMAGQGIVV EILQMSQLRG YRTGGTIHLV
VNNQVGFTTP PGEGRTSIYS TDVAKTIQAP IFHVNGDDPE AVLRVADLAF AYRQEFHRDV
VIDLICYRRR GHNEGDDPSM TQPLMYNLIE AKRSVRTLYT EALVGRGDIT PEEYEAAHQD
FQDRLERAFA ETHAAQTGSI PIITADDGAV ADLERPDSQQ DDAVGEPEST GVSASVIQLI
GDAHDNPPAG FSVHPKLQAL LKKRVEMSRS GGIDWAYGEL LALGSLLLEG TPVRMAGQDT
RRGTFVQRHA VLHDRENGQE WLPLGNLRDQ QARFWIYDSL LSEYAAMGFE YGYSVERADA
LVLWEAQFGD FANGAQTIVD EFISSAEQKW GQRSGVVLLL PHGYEGQGPD HSSARIERYL
QMCAENNMTV ARPSTPASYF HLLRRQAYAR PRRPLIVFTP KAMLRLRGAT SQVEELTHGR
FEPVIDDVRV SDKAAVKRVV LTSGKIYYDL LAELGKRDNQ DSIAIVRIEQ FYPMPITELN
SVLEQYPNAD LIWAQDEPEN QGAWPFFSLA LSKRVTTREV KVSSRGASAS PATGSNKRSA
QEQTALINRA LTI
//
