ID C0XQK7_CORLD Unreviewed; 1253 AA.
AC C0XQK7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EEI17421.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:EEI17421.1};
GN Name=sucA {ECO:0000313|EMBL:EEI17421.1};
GN ORFNames=HMPREF0298_0727 {ECO:0000313|EMBL:EEI17421.1};
OS Corynebacterium lipophiloflavum (strain ATCC 700352 / DSM 44291 / CCUG
OS 37336 / JCM 10383 / DMMZ 1944).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=525263 {ECO:0000313|EMBL:EEI17421.1, ECO:0000313|Proteomes:UP000006196};
RN [1] {ECO:0000313|EMBL:EEI17421.1, ECO:0000313|Proteomes:UP000006196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700352 / DSM 44291 / CCUG 37336 / JCM 10383 / DMMZ 1944
RC {ECO:0000313|Proteomes:UP000006196};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEI17421.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACHJ01000070; EEI17421.1; -; Genomic_DNA.
DR RefSeq; WP_006840689.1; NZ_GG667194.1.
DR AlphaFoldDB; C0XQK7; -.
DR STRING; 525263.HMPREF0298_0727; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000006196; 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 ECO:0000313|EMBL:EEI17421.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 898..1094
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 22..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 138765 MW; E243C2B1660C46CD CRC64;
MSSDSTFGQN DWLVDEMYQQ YRENPSSVDP EWRELFERNG APQTATGDKN VSPAPSPAKA
GDAKESREKT DPKVARTTGA PSQDGRQTKV DQAAAEAASK RSKVLPKPKQ SPLQKIADVS
VEPGERQLKG IYKAIAKNMD ESLSLPTATS VRDMPVKLMF ENRALVNDHL KRTRGGKISF
THIIGYAIVK AAQLHPGMNV NYKVKDNKPF VVQPEHINLG LAIDLPQKDG SRALVVAAIK
ECEKLSFDKF VDGYEDIVNR ARDNKLTMDD FSGVTIQLTN PGGIGTRHSI PRLTTGIGTI
VGVGAMDYPA EFAGASEDRL AELGVGKLVT LTSTYDHRVV QGAESGEFLR TISQLLIDDA
FWDDIFHAMG IPYSPLRWAQ DLPNSGVNKD TRVMQLIEAY RSRGHLIADT NPLRWEQPGL
PKPDSRDLEM ETHGLTLWDL DRTFHVGGFG GKETMTLREV LSRLRAAYTL HVGAEYTHIL
DRDEREWLRD RIEAGMPKPT SAEQKYILQK LNAAEAFENF LQTKYLGQKR FSLEGAETLI
PLMDAVIDTA AGQGLEEVVI GMPHRGRLNV LFNIVGKPVS TIFNEFEGNM QSAQQGGSGD
VKYHLGFEGE HIQMFGDGEI KVSLAANPSH LEAVDPVMVG IARAKDDLLR HSQGRTDHPI
VPLMLHGDAS FAGLGVVQET LNLSNLPGYS VGGTVHIVVN NQIGFTTTPD SGRSTYYATD
LAKGFDCPVF HVNGDDPEAA AWVAQLATEY RREFGKDVFI DLICYRLRGH NEADDPTVTQ
PLMYEQIQSH PSVRTRYTND LIGRGDITAD EAEIAAQDFH DQLDSVFSDV KANEGKPSEQ
TGITEAQSLT RGLDTNITEE TFARLAEAYA NLPEDFTPNK RLNSVLKKRG ASLTEGDIDW
GWGELLAFGS LAEEGKFVRL AGEDSQRGTF TQRHAVLYDP ETGESFNPLD HNAQEADNGG
RFGVYNSALT EFAGLGFEYG YTVGNTDAVV AWEAQFGDFA NGGQTIIDEY ISSGETKWGQ
LSSLISLLPH GYEGQGPDHS SARIERFLQL VAEGSMTIAQ PSTPANHFHL LRRQALGDMK
RPLIIFTPKS MLRNKAAVSQ PADFIEVNRF QSVIDDPFFV ARGNKKVDGA DHSKVTTILL
CSGKIYWELD KRRQKDKRDD VAIIRIEMLH PIPFNRLSDA FANYPNAKQI RFVQDEPANQ
GPWPFYSEHL RNFVDNMPEM VRVSRRSQST TATGVAKVHQ QEEQQLIDEA FAD
//
