ID A0A1Y2R562_9BURK Unreviewed; 963 AA.
AC A0A1Y2R562;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=CAP37_06905 {ECO:0000313|EMBL:OSZ75154.1};
OS Hydrogenophaga sp. IBVHS1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985169 {ECO:0000313|EMBL:OSZ75154.1, ECO:0000313|Proteomes:UP000194358};
RN [1] {ECO:0000313|EMBL:OSZ75154.1, ECO:0000313|Proteomes:UP000194358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS1 {ECO:0000313|EMBL:OSZ75154.1,
RC ECO:0000313|Proteomes:UP000194358};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-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:OSZ75154.1}.
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DR EMBL; NFUU01000001; OSZ75154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2R562; -.
DR STRING; 1985169.CAP37_06905; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000194358; 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 Reference proteome {ECO:0000313|Proteomes:UP000194358};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 607..804
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 963 AA; 106829 MW; 02904D106350F4F1 CRC64;
MSDSSSNGGN VYVAYKGNSY LFGGNAPYVE EMYENYLENP GSVPENWRGY FDALQHVPAG
DGSDARDVPH QPVINAFAER AKQGGTKVVV ATGADSELGR KRVAVQQLIA AYRNVGARWA
DLDPLKRAER DHIPELELSF YGFADADLET VFNTSNTFFG KETMSLRELL NALRETYCGS
IGAEYMYITD QGQKRWWQER LEASRTKPAF NAEKKKHILD RLTAAEGLER FLHTKYVGQK
RFSLEGGESF IASMDELIRQ AGQVGIQEIV IGMAHRGRLN VLVNTLGKMP KDLFAEFDHT
APEELPSGDV KYHQGFSSDV TTPGGPVHLS LAFNPSHLEI VNPVVEGSVR ARMDRRGDPL
GKQVLPVLVH GDAAFAGQGV VMETLALAET RGYSTGGTVH LVINNQIGFT TSDPRDSRST
LYCSDVVKMI EAPVLHVNGD DPEAVVFATQ LALDFRMAFQ KDVVVDIVCF RKLGHNEQDT
PSLTQPLMYK KIAAHPGTRK LYADKLAAQG LGDTLGDDMV KSYRAALDAG RHTVDPVLTN
FKSKFAVDWS PYLGKKWTDN ADSAIPMAEW KRLSDRLTTI PGSVTPHQLV KKVYADRAAM
GRGEIPVDWG MGEHMAFASL VASGFPVRLS GEDCGRGTFT HRHAVIHDQN REKYDEGTYV
PLQNVADNQA PFMVIDSILS EEAVLGFEYG YASNDPNTLV IWEAQFGDFV NGAQVVIDQF
IASGEVKWGR VNGITLMLPH GYEGQGPEHS SARLERFMQL AADTNMQVVQ PTTASQIFHV
LRRQMIRGLR KPLIIFTPKS LLRNKDATSP LSEFTKGGFQ TVIPEHDADV VKKAEKVKRV
ICCSGKVYYD LVKKREERGS DDVAILRVEQ LYPFPHKVFG AEMRKYPNAT DVVWCQDEPQ
NQGAWFFVQH YIHENMLEGQ KLGYAGRAAS ASPAVGYAHL HQEQQKTLIE AAFGKLKGFI
LTK
//
