ID A0A022LMJ6_9ACTN Unreviewed; 1291 AA.
AC A0A022LMJ6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Alpha-ketoglutarate decarboxylase {ECO:0000313|EMBL:EYT63367.1};
DE EC=4.1.1.71 {ECO:0000313|EMBL:EYT63367.1};
GN Name=kgd {ECO:0000313|EMBL:EYT63367.1};
GN ORFNames=H483_0108115 {ECO:0000313|EMBL:EYT63367.1};
OS Dietzia sp. UCD-THP.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1292020 {ECO:0000313|EMBL:EYT63367.1, ECO:0000313|Proteomes:UP000019757};
RN [1] {ECO:0000313|EMBL:EYT63367.1, ECO:0000313|Proteomes:UP000019757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THP {ECO:0000313|EMBL:EYT63367.1,
RC ECO:0000313|Proteomes:UP000019757};
RX PubMed=23661480;
RA Diep A.L., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft Genome Sequence of Dietzia sp. Strain UCD-THP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00197-E00113(2013).
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:EYT63367.1}.
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DR EMBL; AOSR01000024; EYT63367.1; -; Genomic_DNA.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000019757; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:EYT63367.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 947..1140
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 23..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..884
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 142338 MW; 4819F0EF8C9DB0E7 CRC64;
MSKTVSQFGQ NQWLVDEMYE RFSKDPSSVD KSWHEFFDAN PGAATGRDAS TGSSGAGAAS
GGGGTRTGGK NGDEKNGGAK KGKKVSADTS GGDNATPDAN TQKTSELTVA DVSPESSAKD
VAAKPADDST PARKARGQGV PAPVRSTETR KRSEAPAAKR TTKPEYTPPE EPENKVLRGP
ANAIVKNMNA SLALPTATSV RAVPAKLMID NRIVINNHLK RTHGGKISFT HLIGYAMVQA
VKAYPNMNNY FEEIDGKPNV VTPNGINLGL AIDMKTKAGR TLVVAAIRNC EKLDFRGFLD
AYEDIVSRAR VGKLTMEDFS GVSISLTNPG GIGTVHSVPR LTPGQGAILG VGAMEYPAEF
QGASDEQLAN NAIGKITTLT STYDHRIIQG AESGEFLREI HRLLLADEFY DEIFDVLGIP
YEPVRWRQDI TDPRVDKDAR VLELIAAYRD RGHLMADIDP LDGRHAQRRR TFHPDLDVNS
HELTLWDLDR KFSVGGFVGK DKMRLRDVLS ALRAAYCRKI GIEYTHILEN DQRQWIQDRL
EGVDDKPTVA EQKYILSKVN AAEAFETFLQ TKYVGQKRFS LEGAESVIPM MDAVIDEAAE
FALDEVVIGM PHRGRLNVLA NIVGKPYRQI FTEFEGNMDP SAAHGSGDVK YHLGAEGIQY
QMFGENEIKV SLTANPSHLE AVDPVLEGIV RAKQDLIEDP EWRAEYPVVP LMLHGDAAFA
GQGVVAETLN LSQIDGYRTG GTIHIVVNNQ IGFTTAPEAG RSSQYATDVA KMIGSPIFHV
NGDDPEACVR VARLAMDFRQ QFKKDVVIDL VCYRRRGHNE ADDPSMTQPR MYEVIDAKKS
VRQSYTDDLV GRGDITEKEA ENALRDFQGQ LERVFNEVRE LEKHPVKASE SILPNQPLPK
RLVTAVDESV IHAIGDAFGN LPEDFHIHSR VKPVYEARQK MAYNGNIDWA FAELLAIGSL
VQEGRTVRLA GQDSQRGTFT QRHAVVVDKT TSEPYSPLQN LEDAEGRFEV WNSALTEFAG
VGFEYGYSVG DPEALVLWEA QFGDFVNGAQ TIIDEYISSG EAKWGQKSSV TLLLPHGHEG
MGPDHTSGRM ERFLQLCAEG SMTVAQPSTP ANYFHLMRRH ATDGIKRPQI VFTPKSMLRN
KKAVSALEDF TTGKFRSVLD DPTFVDGGKD PEKVTTMLLV SGKLYYELAA RQEKEGHDHI
AIVRLEQIHP IPFRRLREAL GHYPNLSEVR WVQEEPANQG AWSFLALNLP EVIPEFPPIK
RVSRRAMAAT STGLSKVHAV EQKALVDEAF S
//
