ID A0A1J5BTP9_9BURK Unreviewed; 669 AA.
AC A0A1J5BTP9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE Flags: Fragment;
GN Name=sucA {ECO:0000313|EMBL:OIP14845.1};
GN ORFNames=AUK50_11320 {ECO:0000313|EMBL:OIP14845.1};
OS Comamonadaceae bacterium CG2_30_57_122.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1805089 {ECO:0000313|EMBL:OIP14845.1, ECO:0000313|Proteomes:UP000182154};
RN [1] {ECO:0000313|EMBL:OIP14845.1, ECO:0000313|Proteomes:UP000182154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_57_122 {ECO:0000313|EMBL:OIP14845.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP14845.1}.
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DR EMBL; MNXW01000255; OIP14845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5BTP9; -.
DR Proteomes; UP000182154; 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; 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; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
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; PF02779; 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 15..52
FT /note="2-oxoglutarate dehydrogenase E1 component N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16078"
FT DOMAIN 222..506
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT DOMAIN 602..650
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
FT NON_TER 669
FT /evidence="ECO:0000313|EMBL:OIP14845.1"
SQ SEQUENCE 669 AA; 74276 MW; 51441635589C9A90 CRC64;
MSETNSVYQA YQANTYLFGG NAPYVEEMYE NYLANPGSVP DTWRDYFDAL QHVPAVDGSN
AKDVPHQPVI DAFAQRAKAG GTKVVMASED AEMGRKRTAV QQLIAAYRNV GAGWADLDPL
KRTERRDIPE LDPAFYGFTD ADQEVIFDTS NTFFGKDKMP LRELLNALRE TYCSSIGAEY
QYLTDQTQKR WWQQKLESVR SKPSFNTEQK KHILDRLTAA EGLERFLHTK YVGQKRFSLE
GGESFIAAMD ELVQKAGLQG VQEIVIGMAH RGRLNVLVNT LGKLPADLFA EFDHTAPEEL
PSGDVKYHQG FSSDVTSPGG PVHLTLAFNP SHLEIVNPVV EGSVRARMDR RADPTGRQVL
PVLVHGDAAF AGQGVNQETL ALAQTRGYTT AGTVHIIINN QIGFTTSDPR DMRSTLYCTD
IVKGVEAPVM HVNGDDPEAV VMAMQWALEY RMEFRKDVVL DIICFRKLGH NEQDTPALTQ
PLMYKKIAAH PGTRKLYADK LSAQGLGATL GDDMFKAYRV AMDAGKHTVD PVLTNFKSKY
AVDWSPFLGK KWTDAGDTAI PMAEWKRLAE KITTIPASVH PHPLVKKVYD DRAAMGRGDI
PVDWGMGEHM AFASLVASGY PVRLSGEDCG RGTFTHRHAV IHDQSREKWD VGTYVPLQNV
AENQASFSV
//
