ID G8RJE8_MYCRN Unreviewed; 649 AA.
AC G8RJE8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:AEV74699.1};
GN OrderedLocusNames=MycrhN_4197 {ECO:0000313|EMBL:AEV74699.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74699.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV74699.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV74699.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003169; AEV74699.1; -; Genomic_DNA.
DR RefSeq; WP_014212449.1; NC_016604.1.
DR AlphaFoldDB; G8RJE8; -.
DR STRING; 710685.MycrhN_4197; -.
DR KEGG; mrh:MycrhN_4197; -.
DR PATRIC; fig|710685.3.peg.4211; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_11; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000005442; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT DOMAIN 28..215
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 267..477
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 517..596
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 649 AA; 68936 MW; CAEBF017A944B467 CRC64;
MGANGSGANP ATRQKLEKVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA TQPNYPAEIR
APQGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANVNDLPRGG LIIANSDEFT
KRNLAKVGYE GNPLENEDLS DYVVQAVPMT TLTLGAVEEI GASKKDGQRA KNMFALGLLS
WMYGRELEHS EAFIREKFAR KPDIAEANVL ALKAGWNYGE TTEAFASSVY EVAPAKLKSG
EYRQISGNTA LAYGIVTAGQ LSDLQVVLGT YPITPASDIL HELSKHKNFN VLTFQAEDEI
AGIGAAIGAS YGGALGVTST SGPGISLKSE AMGLAVMTEL PLIVIDVQRG GPSTGLPTKT
EQADLLQVLF GRNGESPVAV VAPRSPSDCF DVAVEAVRIA ITYHTPVVIL SDGAIANGSE
PWQIPDVSTY EKIEHTFAKT GEPFQPYARN PETLARQFAI PGTPGLEHRI GGLEAANGSG
NISYEPKNHD LMVRLRQAKV DGIAVPDLEV DDPTGDAELL MLGWGSSYGP IGEACRRARR
NGIKVAQAHL RNLNPFPANL GEVLRRYPNV VLPEMNLGQL ALLLRGKYLV DVQSVTKVEG
MAFLADEVEG IIDAALDGTL GDKEIDKAKF ARLAAATIES EANGVGAIA
//
