ID A0A0Q6LE93_9BURK Unreviewed; 952 AA.
AC A0A0Q6LE93;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:KQU66048.1};
GN ORFNames=ASC88_10735 {ECO:0000313|EMBL:KQU66048.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU66048.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU66048.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU66048.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU66048.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU66048.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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:KQU66048.1}.
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DR EMBL; LMCN01000043; KQU66048.1; -; Genomic_DNA.
DR RefSeq; WP_056808767.1; NZ_LMCN01000043.1.
DR AlphaFoldDB; A0A0Q6LE93; -.
DR STRING; 1736511.ASC88_10735; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000051195; 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:KQU66048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 598..795
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 952 AA; 105901 MW; E3021EEEF3FEB50A CRC64;
MMQEYRSNSY LFGGNAPYVE EMYEAYLDNP GSVPDNWRAY FDALQHVPAA DGSSAADVPH
APVVESFAQR AKANAFGNKA SSADLAVARK QVHVQSLIAA YRVLGARWAD LDPLKRVERP
KIPELEPAFY DLSESDMDIT FSATNTYFST SEQMTLRQIV QALRETYCGS IGAEYMHITD
QPEKRWWQQR LEAIRSKPNF TAEQKKQILN RLTASEGLER YLHTKYVGQK RFSLEGGESF
IASMDELVQR AGEKGVQEIV IGMAHRGRLN VLVNTLGKMP KDLFAEFDHT APENLPSGDV
KYHQGFSSDV TTDGGPVHLS LSFNPSHLEI VNPVVEGSVK ARLDRRGDKE GDTVLPVLVH
GDAAFAGQGV VMETLALAQT RGYYTGGTVH VVINNQIGFT TSDPRDTRST LYCTDVVKMI
EAPVLHVNGD DPEAVVLCTQ LALDYRQEFN KDVVVDIVCF RKLGHNEQDT PALTQPLMYK
KIAQHPGTRK LYGDKLVAQG VLPADGPDAM VKEFRAAMDA GKHTIDPVLT NYKSKYAVDW
SPYLNKKWTD SADTALPLAE VKRLAERITT VPANFKPHPL VEKVLADRAA MGRGDINMDW
GMGEHLAFAS LVASGYPIRL SGEDSGRGTF THRHAVLHDQ NREKWDEGTW TPLQHVADNQ
APFVVIDSLL SEEAVLGFEY GYASADPNTL TIWEAQFGDF VNGAQVVIDQ FIASGEVKWG
RANGLTLMLP HGYEGQGPEH SSARLERFMQ LAADNNMQIV QPTSASQIFH VLRRQMVRMF
RKPLVIMTPK SLLRNKDATS PLVEFTKGEF KTVIPEANAE IAADKVKRIV ACSGKVYYDL
VKARAEKKAT DVAIIRVEQL YPFPHKAFAA EVKKYANATE IVWCQDEPQN QGAWFFVQHY
IHENMVDGQR LGYAGRPASA SPAVGYAHLH QEQQKALLDQ AFAKLKGFVL TK
//
