ID A0A1V3Q010_9GAMM Unreviewed; 948 AA.
AC A0A1V3Q010;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=B0E48_11220 {ECO:0000313|EMBL:OOG56672.1};
OS Rhodanobacter sp. C03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945858 {ECO:0000313|EMBL:OOG56672.1, ECO:0000313|Proteomes:UP000189128};
RN [1] {ECO:0000313|EMBL:OOG56672.1, ECO:0000313|Proteomes:UP000189128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C03 {ECO:0000313|EMBL:OOG56672.1,
RC ECO:0000313|Proteomes:UP000189128};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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 -!- 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:OOG56672.1}.
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DR EMBL; MUNT01000006; OOG56672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3Q010; -.
DR STRING; 1945858.B0E48_11220; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000189128; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 599..791
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 948 AA; 104638 MW; FE434B4A02E0C7D8 CRC64;
MSTNLIREFF DSSQLAGGNA DYVESLYDAW LADATSVPAE WSKYFETFKG RESGDVSHVP
AIARIEAAQK QRHVGNGAAA APISDEHARK QAGVLRLLTA YRSRGHLAAD LDPLGLTEKM
SAPDLGLAFH GLSDADLDTE FDTGNYAGGG QRLKLRELLS RLQKTYASTI GTEFMHISNH
EQRNWIYSRL EQAAGKSTLD KAGKQRVLDG LTAAEGLERY LHTKYVGQKR FSLEGGDSLI
PMIDDVVRAA GDNGIKELVI GMAHRGRLNV LVNILGKPPK TLFDEFEGKF EHPDDPAHSG
DVKYHMGFSA DVKTPKGGVH VALAFNPSHL EIVNPVVCGS VHARQTRRRD TMHTQSMAVL
IHGDAAFAGQ GVNMELLNMS QARGFKIGGS LHIVINNQVG FTTSNPQDAR STMYCTDLAK
MVNAPVLHVN GDDPEAVIAV TRLAYDFRKQ FRRDVVIDLV CYRRHGHNEA DEPAATQPVM
YKIIRARPTA RDLYQQQLVK EGVLAEGDAQ KQFEAYRDRL EAGAPMTELD PSPTRDGHVD
WAKFIGGKLS TPTDTSVPKQ KLQELSSKIL TLPADITLQA RVAKIYDDRR KMAAGEQPAD
WGFAENLAYA TLIDAGHDMR LVGQDSGRGT FFHRHAVLHD QKDGHTYMPL ATIRAGADVE
VIDSLLSEEA VMAFEYGHST TDPDTLNIWE GQFGDFANGA QVVIDQFISS GEAKWNRLCG
LALFLPHGYE GQGPEHSSAR LERFLQLCAF DNMQVCVPTT PAQDFHMIRR QMLRPVRKPL
IVMTPKSLLR HKLAVSSLDE LANGSFQLVI GEHRELPAKK VKRVVLCSGK VYYDLLEDAE
KRGSNDVTIV RVEQLYPFPR VEVTAELDKY PSAKEVIWCQ EEPMNQGAWF QIRHHLQACT
GSKRSLSYAG RARSPAPAAG HLNTHVAEQA ALVEQALVAP VGTDHSAE
//
