ID A0A2T7TKF1_9MICC Unreviewed; 1314 AA.
AC A0A2T7TKF1;
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=Multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit {ECO:0000313|EMBL:PVE18522.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:PVE18522.1};
GN Name=kgd {ECO:0000313|EMBL:PVE18522.1};
GN ORFNames=DDA93_08255 {ECO:0000313|EMBL:PVE18522.1};
OS Arthrobacter sp. Bz4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=2171979 {ECO:0000313|EMBL:PVE18522.1, ECO:0000313|Proteomes:UP000244710};
RN [1] {ECO:0000313|EMBL:PVE18522.1, ECO:0000313|Proteomes:UP000244710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bz4 {ECO:0000313|EMBL:PVE18522.1,
RC ECO:0000313|Proteomes:UP000244710};
RA Goncharov A., Nikolskiy P., Shidlovsky F., Kolodzhieva V., Zueva L.,
RA Masharskiy A., Suvorov A.;
RT "Putative ancient Arthrobacter sp. strain from the intact mummy of late
RT pleistocene steppe bison (Bison priscus bojanus).";
RL Submitted (APR-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:PVE18522.1}.
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DR EMBL; QDAE01000008; PVE18522.1; -; Genomic_DNA.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000244710; Unassembled WGS sequence.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 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 Lyase {ECO:0000313|EMBL:PVE18522.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244710};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000313|EMBL:PVE18522.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 975..1168
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 46..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 145107 MW; 4BEE0B382C096281 CRC64;
MPEQPNHRLP EEFGGNEWLV DELYEKFQQD RNSVDKKWWT LFDSFAADDS KSENGRHTAP
RAATASANTS SVDNSSVNNG SVANSSGDLG HNPATRELPV VNAESNSPKS SGESPASFEE
SAKPPVPKET HSKAEVRAED NADRAIEKAA QERAEKPVSR QSDNAKAEKP STTPIPAQLP
KSDRTTEMDE DTVKVLRGPA KAIATNMDAS LTVPTATSVR AIPAKLLIDN RVVINNHLAR
ARGGKVSFTH IIGYAIIRAL AQFPSQNVYY DVVDGKPAAV QPAHVNFGLA IDMPKPDGTR
LLVVPNIKKA ETMNFSDFWH AYEELVKKAR GGKLGADDYA GTTVSLTNPG GIGTVHSVPR
LSKGQACIIG AGALEYPAEF QGSSEKTLAQ HAISKTITLT STYDHRVIQG AGSGEFLRII
HQLLLGEQNF YDEIFEALRI PYEPVRWSAD IQVDPMDEIN KVARIQQLIH AYRVRGHLMA
DTNPLEYVQR KHADLDVRTH GLTLWDLDRE WPTGGFGGKP MLKFRTILGV LRDAYCRTTG
IEYMHIQDPE ERQWFQDELE HSYSKPSREE QMRVLHQLNA AEAFETFLQT KFVGQKRFSL
EGGESLIPLL DSIISNAADD GLDEVAIGMA HRGRLNVLTN IAGKTYGQVF REFEGTQDPR
SVQGSGDVKY HLGTEGTFTS DSGNETKIYL AANPSHLEAV DSVLEGIVRA KQDRLDLGDA
FPVLPIQIHG DAAFAGQGVV AETLNLSQLR GYRTGGTIHI IVNNQVGFTT SPTSSRSSVY
STDVAKMVQA PIFHVNGDDP EAVVRVGQLA YQFRQKFNKD VVIDMVCYRR RGHNEGDDPS
MTQPMMYNLI EAKRSVRKLY TEALIGRGDI SQDEAEQALR DYQERLERVF AETHAAQTSP
IPIVTKDAAA VSDIERPLSQ QSDTGVGVPA STAITPETLA HIGKVHTAVP ENFTVHPKLK
ALLDKREQMS REGGIDWGFG ELAAFGSLLM EGVPVRLAGQ DSRRGTFVQR HAVFHDRATG
EEWLPLDDLS DAQAKFWIYD SLLSEYAAMG FEYGYSVERP DALVLWEAQF GDFVNGAQTI
IDEFISSAEQ KWGQRSSLVL MLPHGYEGQG PDHSSARIER FLQMCAEDNM VVANPTSAAS
HFHLLRRQAY TRPRKPLIIF TPKQLLRLKA AASSVEDFTN GTFLPVIPDK QEPNAKDVDH
VILVSGRLYY DLLASRQKTE DQKSAIIRVE QLAPLPVEDI KAAVGKYPNA DLVWAQDEPA
NQGPWPFIGL NLPEHLDRPL HLASRPASAS TATGSAKRHA VEQEILVKKA FERQ
//
