ID D7WDL8_9CORY Unreviewed; 1284 AA.
AC D7WDL8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EFK54249.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:EFK54249.1};
GN Name=sucA {ECO:0000313|EMBL:EFK54249.1};
GN ORFNames=HMPREF0291_11906 {ECO:0000313|EMBL:EFK54249.1};
OS Corynebacterium genitalium ATCC 33030.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=585529 {ECO:0000313|EMBL:EFK54249.1, ECO:0000313|Proteomes:UP000004208};
RN [1] {ECO:0000313|EMBL:EFK54249.1, ECO:0000313|Proteomes:UP000004208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33030 {ECO:0000313|EMBL:EFK54249.1,
RC ECO:0000313|Proteomes:UP000004208};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) 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:EFK54249.1}.
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DR EMBL; ACLJ02000003; EFK54249.1; -; Genomic_DNA.
DR STRING; 585529.HMPREF0291_11906; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000004208; Chromosome.
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 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 ECO:0000313|EMBL:EFK54249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004208};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 931..1127
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1284 AA; 141807 MW; B94E9253F9FBF687 CRC64;
MASTARDGAD PIKQTDYTEN NKEARRATAV SSENTFGQND WLVDEMFQQY QEDPNSVDEE
WRELFDKKGT PDSGAPLASP AAKKAAADSG SNDRPHRART ETKVAETTGA PSQDGRETKV
DKAIETTAKS QPSEKNAAKK TPKPSPMEKV KPLPEAGETQ LKGTFKAIAK NMDESLTVPT
ATTVRDMPVK LMFENRAQIN DHLKRTRGGK ISFTHIIGWA IVKSAMIHPG MNVNYTVKDG
KPFVVTPEHI NLGLAIDLPQ KDGTRALVVA AIKECETLTF EQFVRAYEDI VARARDNKLK
IDDFQGVTIQ LTNPGGIGTR HSIPRLTKGQ GTIVGVGAMD YPAEFAGASE DRLAELGVGK
LTTLTSTYDH RVIQGAESGE FLRDISQLLI DDKFWDEIFD AMSIPYAPMR WAQDIPNTGV
DKSTRVMNLI EAYRSRGHLI ADTNPLNWEQ PGLPKPDVSD LLLETHGLTL WDLDRTFNVG
GFGGKETMTL REVITRLRAA YTLHVGAEYT HVLDRDERDW LRDRLEVGMP KPTNAEQKYI
LQKLNAAEAF ENFLQTKYLG QKRFSLEGAE TLIPLMDAVI DTAAGQGLDE VVIGMPHRGR
LNVLFNIVGK PVKTIFGEFE GNLQPAQQGG SGDVKYHLGF EGEHIQMFGD GDIKVSLAAN
PSHLEAVDPV LVGIARAKQD IINHGQPADD HPIVPMMLHG DASFTGLGVV QETLNMSKLT
GYDVGGTVHI VVNNQVGFTT TPDQGRSTYY ATDLAKGFDC PVFHVNGDDP EAAAWVGQLA
TEYRREFGKD VFIDLICYRL RGHNEADDPS VTQPVMYERI DSHPSVRTRY TKDLIGRGDI
TEEEAEIAAQ DFHDQLDSVF NDVKEGGGSP AEQTGITESQ ELTRGLDTSI DEDLFKKLAD
AYANLPDDFT PNKRLKTVLK ARGGSFDGGD IDWAWGELLA FGSLAHGGKL VRLAGEDSKR
GTFTQRHGVL FDPSTAEQYN PLDAIAIEAG NGGRFQIYNS ALTEFGGLGF EYGYTVGNPD
ALVAWEAQFG DFANGGQTII DEYISSGETK WGQLSSLIML LPHGYEGQGP DHSSARIERF
LQLVAEGSMT IAQPSTPANH FHLLRRQALG EMRRPLVIFT PKSMLRNKAA VSQPAEFIET
TGFRSVIDDP HLVDANNKVI GDAEKVKTIM LCSGKIYYEL EKRRQKDGRD DVAIIRIEML
HPIPFNRLSD AFANYPNAEE IRFVQDEPAN QGPWPFYNEH LANYVENMPP MRRISRRSQS
TTATGVSKVH QQEEKALLDE AFAD
//
