ID F9PN32_9ACTO Unreviewed; 1275 AA.
AC F9PN32;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=2-oxoglutarate decarboxylase {ECO:0000313|EMBL:EGV12423.1};
GN ORFNames=HMPREF9058_0916 {ECO:0000313|EMBL:EGV12423.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV12423.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV12423.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV12423.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV12423.1}.
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DR EMBL; AFUR01000006; EGV12423.1; -; Genomic_DNA.
DR RefSeq; WP_009407412.1; NZ_AFUR01000006.1.
DR AlphaFoldDB; F9PN32; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000004281; 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 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 929..1122
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 24..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 139126 MW; 23B63670C4FE6DA1 CRC64;
MPTQDQISPG FGANEWMVEE MRAAWSADPS SVSPQWRELF ETDPSAGLHQ PGPASSNGSA
SSAAGGPRRA TITPQAASSL RRSSAVQDVT RSDLPPAPPS DTAPPTSPYA QRQAGHPAHD
QDGDAYEDRT TRLKGAAART AKNMDDSLSM PTATSARAVP AKVLIENRAV INTHLARTRG
GKVSFTHLIG WAVVESLTEM PSMNVSYGVD EAGKPVLHEP AHVAFGLAID VPGSDGQRRL
LVPSIKQADL MDLSQFVEAY EALVAKAREN KLDLDDFRGT TVTLTNPGMI GTLHSVPRLM
PGQGLIVGVG AMDYPAAFAG ASPDTLARQA IGKVVTLTST YDHRVIQGAA SGEFLRLVER
KLLGLDGFWN RAFESLRIPL EPVKWVRDTT YDPELETGKP ARVAELIHAY RQRGHLAADN
DPLTYRLRRH PDLDITSYGL SLWDLDRSFP TRGLGGRDRA TLREILRMLR DAYCRTVGVE
YMHIQDPAQR AWWQERLERD WEDIADEERR RILTKLEQAE AFETFLQTKY VGQKRFSLEG
GESLIVALDR LLDAAAHDGL DEVVIGMAHR GRLNVLTNIA GKSYGQVFDE FEGNGVIEGA
GTGDVKYHLG TVGVFSGTDG VSTRVSLAAN PSHLETVDGV VEGIVRAKQD RIGLGEKGYT
VMPVLVHGDA AFAGQGVVYE TLNMSQLPAY RTGGTVHIVV NNQIGFTTGS ASARSTIYAT
DLAKGLQVPI FHVNADDPET VARTARHAYE YRRTFHKDVI IDLICYRRRG HNEGDDPSMT
QPLMYRLIDS LDSTRGVYTA ALVGRGDITP QEAQEIAKSY QDELERVFAE ARVQVTGGTG
SDGAGEAADT ATQDLSDPTK VGVPLSSLEI PYSQRAGTGM MLGWTSAVPR DVVERIGDAQ
VAWPESFTVH PKLQAMLSKR REATREGGID WGLGELIALG SLLMEGVPIR LAGEDARRAT
FAQRHAVLHD HTSGQEWTPL SFLTPDQAPL EIYDSLLSEY AALAFEYGYS VERPEGLTMW
EAQFGDFANG AQSVIDEYVT SAAQKWGQRS GLVMLLPHGQ EGQGPDHSSA RIERYLQMCA
QDNMLVAQPS TPASYFHLLR EHTYTRPRRP LIVFTPKQLL RLKAACSPVE DFTSGTFQPV
IGETDDAVLA TARKQGVDRV LLCSGRVYYD LLAHRTKTGD TSTAIVRLEQ LYPLESSDIA
EALAPFSGAE LVWVQDEPAN QGMWPYLALN LPTDLTGGVL PTLVSRPEAA APAVGTAGVH
RAQQEEILRQ AFARH
//
