ID A0A086Y607_9RHOB Unreviewed; 987 AA.
AC A0A086Y607;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:KFI29707.1};
GN ORFNames=CG50_08720 {ECO:0000313|EMBL:KFI29707.1};
OS Paenirhodobacter enshiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paenirhodobacter.
OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI29707.1, ECO:0000313|Proteomes:UP000028824};
RN [1] {ECO:0000313|EMBL:KFI29707.1, ECO:0000313|Proteomes:UP000028824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI29707.1,
RC ECO:0000313|Proteomes:UP000028824};
RA Wang D., Wang G.;
RT "Genome of Paenirhodobacter enshiensis DW2-9.";
RL Submitted (MAR-2014) 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:KFI29707.1}.
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DR EMBL; JFZB01000003; KFI29707.1; -; Genomic_DNA.
DR RefSeq; WP_036634772.1; NZ_JFZB01000003.1.
DR AlphaFoldDB; A0A086Y607; -.
DR STRING; 1105367.CG50_08720; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000028824; 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:KFI29707.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028824};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 634..827
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 987 AA; 109577 MW; E5C65A4F37E430B7 CRC64;
MNDQSSNEAF EASSFLQGAN ADYVEQLYAN YAKDPASVDA SWQAFFASLG DAETDVKHAA
NGPAWTRTDW PQSPSGELIG ALTGEWPAVP AKEAKAAGDK IKAKAADAGV QISEEQVQRA
VLDSVRAIMI IRAFRIRGHL IADLDPLHMR PEEVVHYPEL DPASYGFTAA DMDRPIFIDN
VLGLVHASMH QILDILKRTY CGTFALQYMH ISNPEESAWL KERIEGYGKE IQFTREGRRA
ILNKLVEAEG FEKFLHVKYM GTKRFGLDGG EALIPAMEQI IKRGGALGMK EMVIGMPHRG
RLNVLTNVMG KPFRAIFNEF QGGSYKPDDV DGSGDVKYHL GTSSDRTFDG NTVHLSLVAN
PSHLEAVNPV VLGKVRAKQD QLNDTDRTQV LGVLLHGDAA FAGQGIVAEC FQLSGIRGHR
TGGTIHIVVN NQIGFTTAPH FSRSSPYPTD IALMVEAPIF HVNGDDPEAV VHAAKVATEF
RQKFHKDVVL DIFCYRRFGH NEGDEPMFTN PLMYKAIKGH KTTLQLYTDR LVKDGLIPEG
EIEDMKASFQ SMLNGEFEAG KTFKPNKADW LDGKWTGMQP EGREYTPGDT AVSPETFAEV
GKALVSYPDG FDLHKTVKRN LEHKAKMFET GEGFDWATGE ALAYGSLLAE GHGVRLSGED
SARGTFSQRH SALIDQTTEE RFYPLNHIKP GQAHYEVIDS ALSEYAVCGF EYGYSLAEPN
TLTLWEGQFG DFANGAQIIF DQFVSSGESK WLRMSGLVLL LPHGYEGQGP EHSSARLERY
LQMSAQDNWI VANVSTPANY FHILRRQIKR SFRKPLVLMT PKSLLRHPLC VSKAEEFTTG
STFHRVLHDD AERGYSATQL KPDAEIKRVV ISSGKVYYDL LAERDARGLT DVYLLRLEQF
YPFPAKSLER ELSRFKGAKV IWCQEEPKNM GGWTFVEPNI EEVLVKIGAT HNRPRYAGRV
ASASPATGLA KIHKAEQEAL VNEALEG
//
