ID A7H8J4_ANADF Unreviewed; 940 AA.
AC A7H8J4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Anae109_0829 {ECO:0000313|EMBL:ABS25040.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25040.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS25040.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25040.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP000769; ABS25040.1; -; Genomic_DNA.
DR RefSeq; WP_011985146.1; NC_009675.1.
DR AlphaFoldDB; A7H8J4; -.
DR STRING; 404589.Anae109_0829; -.
DR KEGG; afw:Anae109_0829; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_7; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000006382; Chromosome.
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:UP000006382};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 587..780
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104045 MW; 4F87C38514A594AF CRC64;
MSSPETELPV PAPSASNLSF VEDLYYEWLA DPSAVDERWR RYFESVPATP GTAKAPEAFA
PRRPDGGVAP APGAALASAD AAFQAKVDRL VTAYREYGHL RADLDPLALT RRAERFSPAT
FGLSDAELER PCADPEGRGD RTLRGLVARL EETYCRTLGV ELAHMHDADL RGWLEQRMER
TRNRVSLEPE VKRRLLEKVV EAETLEQYLG TKFLGAKRFS VEGAEGLLPL FELAVDRAIG
HGVRNVVIGM AHRGRLNVLA NVVGKPLRDI FAEFRDAAII NAGGGDVKYH LGYSSDRESA
EGVLVHLSLA FNPSHLEWID TVVQGRVRAK QDRYRDTDRH RSLPILVHGD AAFAAQGVVA
ESLQMSELEG YAVGGTIHVI VNNQVGFTTS PRDARSTTYA TGPARMLQIP IIHVNGEDLE
AIAQAVLLAV DFRQRFHRDV VIDLWTYRRH GHNEGDEPAF TQPVMYRAIS RKPTLKALYG
QQLVKEGTIA AGEVEQMVAR YRARLEEAYQ ASAKIAVQPG AQAMSGFWKD YRGGPMGREE
PPTGVAPEVL RQVGELLVQL PRGFRVHPKL AKVLEARAQM VRGERPLDWA MAEALALGTL
AWEGARIRLS GQDVRRGTFS HRHSVLYDHE SGVPYSPLSH LRSGQGPVEI RDSLLSEAGA
LGFEYGYSLE MPDALTLWEA QFGDFVNAAQ VIIDQFLSSG EAKWNRLSGL ALLLPHGMEG
QGPEHSSARL ERFLELSVDD NWRVVNLTTP AQYFHALRRQ VRSPFRKPLV VMSPKSLLRH
PQVVSPLDLL ARERFQPVID DESADPTETT RVVLCSGKLY YDLAGARTAQ GARHAAIVRL
EQLYPLDVES VRASIARLRP GVEIVWAQEE PSNMGAWDYV NAHLAPRLPS RVALVARAPS
ASPAAGSATR HRLEQEQLVR EALGEPVSRI RADRAAAQER
//
