ID A0A132T4C2_9MYCO Unreviewed; 654 AA.
AC A0A132T4C2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KWX66220.1};
GN ORFNames=ASJ79_06535 {ECO:0000313|EMBL:KWX66220.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX66220.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX66220.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX66220.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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:KWX66220.1}.
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DR EMBL; LMVQ01000235; KWX66220.1; -; Genomic_DNA.
DR RefSeq; WP_067957422.1; NZ_LMVQ01000235.1.
DR AlphaFoldDB; A0A132T4C2; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000070146; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT DOMAIN 31..218
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 269..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 519..598
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 654 AA; 69437 MW; DE604C899630FF8B CRC64;
MGENGNVAGH VTGAPRQKLE KVVIRFAGDS GDGMQLTGDR FTSEAALFGN DLATQPNYPA
EIRAPQGTLP GVSSFQIQIA DYDILTAGDR PDVLVAMNPA ALKANVSDLP RGGLIIANSD
EFTKRNLAKV GYDANPLEND ELSDYVVQAV PMTTLTLGAV ESIGASKKDG QRAKNMFALG
LLSWMYGREL EHSEAFIREK FARKPDVAEA NVLALKAGWN YGETTEAFGT TYEVSPAKLK
TGEYRQISGN TALAYGLIAA GHLADLQIVL GTYPITPASD ILHELSKHKN FNVLTFQAED
EIAGIGAAIG ASYGGALGIT STSGPGISLK SEAIGLAVMT ELPLIVIDVQ RGGPSTGLPT
KTEQADLLQA MFGRNGESPV ALLAPRSPSD CFDIAVEAAR IAINYHTPVM ILSDGAIANG
SEPWRIPDVS SYERIEHTFA KEGEPFQPYA RDPETLARQF AVPGTPGLAH RIGGLESANG
SGNISYEPKN HDLMVRLRNE KIAGIAVPDL EVDDPTGDAE LLMLGWGSSY GPIGEACRRA
RRNGIKVAHA QLRHLNPFPA NLGEVLNRYA KVVVPEMNLG QLALLLRGKY LVDVQSVTKV
EGMAFLADEV EGIIDAALEG TLGDKEIEKA KFARLAAATI EAPATDATGV GANA
//