ID A0A1C6SBG0_9ACTN Unreviewed; 615 AA.
AC A0A1C6SBG0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:SCL26671.1};
GN ORFNames=GA0070616_3353 {ECO:0000313|EMBL:SCL26671.1};
OS Micromonospora nigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL26671.1, ECO:0000313|Proteomes:UP000199699};
RN [1] {ECO:0000313|EMBL:SCL26671.1, ECO:0000313|Proteomes:UP000199699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL26671.1,
RC ECO:0000313|Proteomes:UP000199699};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMHT01000003; SCL26671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6SBG0; -.
DR STRING; 145857.GA0070616_3353; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000199699; 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; 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; 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:UP000199699}.
FT DOMAIN 20..207
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 255..474
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 615 AA; 65872 MW; A2539B40E0837B2D CRC64;
MNKQIRQLDR VVIRFAGDSG DGMQLTGDRF TSETAQLGND ISTLPNFPAE IRAPAGTLPG
VSSFQVHFAD YDILTPGDAP NVLVAMNPAA LKANLADLPR GADIIVNTDE FTRRNLAKVG
YATSPLDDDS LAGYVVHPVA LTSMTVGALA ENDVSKKDAE RAKNMFALGL LSWMYSRPYE
STLRFLERKF AARPELVAAN VAAFKAGWNF GETTEDFAVR YEVKPARMQP GTYRNITGNA
ALSLGIVAAG VRSGLPVFLG AYPITPASDI LHELSKHKRL GVVTMQAEDE IAAIGAALGA
SYGGALGVTT TSGPGVALKG ETISLAVALE LPLLIVDVQR AGPSTGMPTK TEQADLNMAL
FGRHGEAPVA VIAPKSPADC FHAAIEAARI ALTYRTPVIL LSDNYVANGS EPWLLPDVES
LPDLRVEFAT APNGEDGTTF LPYLRDPETL ARPWAIPGTP GLEHRIGGLE KADKTGDISY
DPANHDYMVR TRAARIETIP VPDVEVDDPD GDARVLVLGW GSTYGPIGAA CRGLRQRGLS
VAQAHLRHLA PMPANLGQVL RSYDRVVIPE MNLGQLAHVI RARYLIDAIG YNQVRGLPFT
AAELETMLEE VLKNV
//
