ID A0A0M2LS95_9SPHN Unreviewed; 994 AA.
AC A0A0M2LS95;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:KKI18362.1};
GN ORFNames=XM50_18000 {ECO:0000313|EMBL:KKI18362.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI18362.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI18362.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18362.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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:KKI18362.1}.
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DR EMBL; LAZX01000094; KKI18362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2LS95; -.
DR STRING; 1642949.XM50_18000; -.
DR PATRIC; fig|1642949.3.peg.1311; -.
DR Proteomes; UP000033997; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
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; 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; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KKI18362.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 627..818
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 74..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 109576 MW; A0AFBEE7101D86E8 CRC64;
MVMGYEGQDF LDVAGGVSPA FIDALYTRYK ASPDSVEPGW RGFFEGLESG TSGPSWRNDR
WPLTTTDDLT AALDPTQMEP APKPAKGGKP APAAAAPAAA APSQDEIVRA AGDAIRAQLL
VRTYRVRGHL AANLDPLGLN TQRELPADLR TEYHGFTDAD IDRPVYLGGT MGLQWATIRE
LVNILRANYC GNVGLEYMHI ADVEERRFLQ ERMEGKDKAI EFTPQGKKAI LNKVIEAEQW
EKFLGRKYVG TKRFGLDGGE SMIPALESVI KYGGAAGVNE IVFGMAHRGR LNVLANVMGK
PLRVIFHEFA GGSANPDDIG GSGDVKYHLG TSTDREFDGV KVHMSLVANP SHLEAADPVV
LGKVRAIQTI AGDLTDHTKS LPVLIHGDAA FAGQGIVWEC LGFSGIRGYN TGGCVHFVIN
NQIGFTTSPQ FARSSPYPSD VAKGVQAPVF HVNGDDPEAV TFATKMAIEF RQKFHRDVVI
DMWCYRRFGH NEGDEPGFTQ PLMYKAIRNH PPVSEIYGKR LIEQKVVDQA WMDENVKQFT
TLLEGEFEAG ASYKPNKADW FAGRWSGLSV PADPETARRS FDTGIEQKLF DSIGRTLTTV
PEDLAIHKTL ARVIDAKRNM FATGENFDWA TGEALAFGSL LSEGFGVRLS GQDSGRGTFS
QRHAVWVDQN DEHKYVPLWN IEHGRFEVLD SPLSEYGVLG FEYGYALADP KTLVLWEAQF
GDFVNGAQIM IDQFIASGEA KWLRANGLVM LLPHGYEGQG PEHSSARPER FLQLCAQDNI
QVANCTTPAN YFHLLRRQMH RSFRKPLIIF TPKSLLRHKL AVSSRADFVG DSHFRRILSD
TNGAADEATK RLVLCTGKVA YDLIEARDAA GDENTQIVRI EQLYPFPTEA LAKRIARMPN
LEDVVWAQEE PRNNGYWFFV EPFIEDALAE AGCAIKRARY AGRAAAASPA TGLMKRHQAE
QGALIADALG HSVREEIRRT RSAETTKKAG KAAS
//
