ID A0A0F4QX01_9GAMM Unreviewed; 937 AA.
AC A0A0F4QX01;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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 ORFNames=TW77_04715 {ECO:0000313|EMBL:KJZ11854.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ11854.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ11854.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ11854.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ11854.1}.
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DR EMBL; JXYA01000007; KJZ11854.1; -; Genomic_DNA.
DR RefSeq; WP_046003814.1; NZ_JXYA01000007.1.
DR AlphaFoldDB; A0A0F4QX01; -.
DR PATRIC; fig|43658.5.peg.984; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000033452; 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:UP000033452};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 594..787
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 937 AA; 105099 MW; 199282BC6F3285B4 CRC64;
MHEGVMKAWL ESSHLYGGNV AYVEDLYEAY LDDAASVPEE WREVFDQLPK VEGVDVDVKH
SEIKSQFADL AKNKHREVIV SAEGAADAKQ VRVLQLINAF RFRGHQNANL DPLGLWQRDR
VRELDLAYHD LDNADLEKEY NVGSFASGQE TMKLKDLYNA LKTTYCGSVG AEYMHITSTE
EKRWLQQRIE STFAQPKFNK ETKLRILKGL TAADGLEKYL GAKFPGAKRF SLEGGDALVP
MLKELVHRAG ESGQEEVVIG MAHRGRLNVL VNVLGKNPQV LFDEFAGKYG ESAGSGDVKY
HMGYSSDFAT QGGNVHMALA FNPSHLEIVN PVVMGSVRAR LDRLNCKSGS KALPITIHGD
SAIAGQGVVQ ETFNMSQTRA YGVGGSIRIV VNNQVGFTTS NQEDTRSTEY CTDIAKMVQA
PIFHVNADDP EAVAFVTQVA LDFRNKFKRD VVIDLVCYRR HGHNEADEPN ATQPLMYQKI
KKHPVPRQIY ADKLVSEGVM SADEAKTLAD DYRNGLDNGQ IVVEEIQPET KHSSDWSKYV
GHDWDTAYEA SVPVEKLKEL SEKISTYPAD HKAQSRVKKI YDDRKTMASG EKLLDWGMAE
TLAYATLVDQ GTDIRLTGQD SGRGTFFHRH AVVHNQADAS TYLPLQNVRD DQGLFEVYDS
VLSEEAVLAF EYGYATAEPT SLVLWEAQFG DFANGAQVVF DQFLSSGEQK WGRLCGLTLL
LPHGYEGQGP EHSSARLERY LQLCADHNMQ VCVPSTPAQV YAMLRRQSVR PLRRPLIVMT
PKSLLRHPLA VSSLEELSEG VFHNMIDEID DINPENVERV VFCSGKVYYE LLQERRKQEL
NNVAIVRVEQ LYPFPHKEMD EIMARYQHVK DFVWCQEEPQ NQGAWYCSQH HFWEAIPSGA
KLTYAGRKAA AAPACGYMST HTKEQNALIA DALTIKK
//
