ID A0A1X2LX14_9MYCO Unreviewed; 653 AA.
AC A0A1X2LX14;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:OSC41717.1};
GN ORFNames=B8W66_07890 {ECO:0000313|EMBL:OSC41717.1};
OS Mycobacterium decipiens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC41717.1, ECO:0000313|Proteomes:UP000193247};
RN [1] {ECO:0000313|EMBL:OSC41717.1, ECO:0000313|Proteomes:UP000193247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC41717.1,
RC ECO:0000313|Proteomes:UP000193247};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OSC41717.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCXP01000006; OSC41717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2LX14; -.
DR STRING; 1430326.B8W66_07890; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000193247; Unassembled WGS sequence.
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}.
FT DOMAIN 38..225
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 275..487
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 526..612
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 69524 MW; 2C92B13A6361CAFE CRC64;
MDPNGSEAGS ESHDVASHAA PDRQRLENVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA
TQPNYPAEIR APAGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANIGDLPLGG
MVIVNSDEFT KRNLTKVGYV TNPLESGELS EYVVHTVAMT TLTLGAVEAI GASKKDGQRA
KNMFALGLLS WMYGRPIETS ENFIREKFAR KPEIAEANVL ALKAGWNYGE TTEAFGTTYE
ISPATLPPGE YRQISGNTAL AYGIVTAGQL ADLPVVLGSY PITPASDILH ELSKHKNFNV
MTFQAEDEIG GICAALGAAY GGALGVTSTS GPGISLKSEA LGLGVMTELP LLVIDVQRGG
PSTGLPTKTE QADLLQALYG RNGESPVAVL APRSPADCFE TALEAVRIAV SYHTPVILLS
DGAIANGSEP WRIPDVTALQ PIKHTFAKPD EPFQPYARDR ETLARQFAIP GTPGLEHRIG
GLEASNGAGD ISYEPTNHDL MVRLRQAKID GIRVPDLEVD DPTGDAELLL IGWGSSYGPI
GEACRRARRR GTKVAHAHLR YLNPFPANLG EVLRRYPKVV APEMNLGQLA QVLRGKYLVD
VQSVTKVKGV SFLADEIGRF IRAALAGRLG ELEQDKTIIA RLSAATVGAR ANG
//
