ID V7JKU2_MYCAV Unreviewed; 656 AA.
AC V7JKU2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:ETA98945.1};
GN ORFNames=O982_08550 {ECO:0000313|EMBL:ETA98945.1};
OS Mycobacterium avium 10-5581.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETA98945.1, ECO:0000313|Proteomes:UP000018557};
RN [1] {ECO:0000313|EMBL:ETA98945.1, ECO:0000313|Proteomes:UP000018557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-5581 {ECO:0000313|EMBL:ETA98945.1,
RC ECO:0000313|Proteomes:UP000018557};
RA Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT "Genome sequence of MAC strains.";
RL Submitted (OCT-2013) 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:ETA98945.1}.
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DR EMBL; AYNT01000090; ETA98945.1; -; Genomic_DNA.
DR AlphaFoldDB; V7JKU2; -.
DR PATRIC; fig|1392000.4.peg.1816; -.
DR Proteomes; UP000018557; 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 43..230
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 279..491
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 531..616
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 69390 MW; 84D4FF460041E1FD CRC64;
MEGNDVDPNG SGAGSDSQNG ASPNGSSRQR LEQVVIRFAG DSGDGMQLTG DRFTSEAALF
GNDLATQPNY PAEIRAPAGT LPGVSSFQIQ IADYDILTAG DRPDVLVAMN PAALKANIGD
LPRGGMVIAN SDEFTKRNLT KVGYVTNPLE TDELSDYVVH SVAMTTLTLG AVESIGASKK
DGQRAKNMFA LGLLSWMYGR PIETSEKFIR EKFARKPEVA ETNVLALKAG WNYGETTEAF
GTTYEVSRAT LPAGEYRQIS GNTALAYGIV AAGQLADIPV VLGSYPITPA SDILHELSKH
KNFNVITFQA EDEIGGICAA IGASYGGALG VTTTSGPGIS LKSEALGLAV MTELPLLVVD
VQRGGPSTGL PTKTEQADLL QALFGRNGES PVAVLAPRSP SDCFETALEA ARIAVSYHTP
VIVLSDGAIA NGSEPWRIPD VSTLPRITHA FAKPDEPFQP YARDPETLAR QFAVPGTPGL
EHRIGGLEAA NGSGNISYEP VNHDLMVRLR QAKIDGISVP DLEVDDPTGD AELLLIGWGS
SYGPIGEACR RARRKGIKVA HAHLRYLNPF PANLGEVLRR YPQVVCPEMN LGQLALLLRG
KYLVDVQSVS KVQGVAFLAD EIGRVIRAAL GGTLAEVEND KTMVARMAAA TVGASA
//