ID A0A1A1YHQ3_9MYCO Unreviewed; 645 AA.
AC A0A1A1YHQ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:OBF30849.1};
GN ORFNames=A5724_22825 {ECO:0000313|EMBL:OBF30849.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF30849.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) 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:OBF30849.1}.
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DR EMBL; LZHZ01000051; OBF30849.1; -; Genomic_DNA.
DR RefSeq; WP_067806139.1; NZ_LZHZ01000051.1.
DR AlphaFoldDB; A0A1A1YHQ3; -.
DR STRING; 1834117.A5724_22825; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000092025; 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:UP000092025}.
FT DOMAIN 28..215
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 266..476
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 516..594
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 645 AA; 68469 MW; 9DF250C0800F386F CRC64;
MGANGNGADP ATRTKLEKVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA TQPNYPAEIR
APQGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANVSDLPRGG LIIANSDEFT
KRNLAKVGYE TNPLETDELS DYVVQPVAMT TLTLGAVEAI GASKKDGQRA KNMFALGLLS
WMYGRELEHS EAFIREKFSR KPDIAEANVL ALKAGWNYGE TTEAFASTYE VSPAKLTSGE
YRQISGNTAL AYGLITAGQL ADIQLVLGSY PITPASDILH ELSRHKNFNV LTFQAEDEIA
GIGSAIGASY GGALGVTTTS GPGISLKSEA IGLAVMTELP LIVVDVQRGG PSTGLPTKTE
QADLLQAMFG RNGESPVAII APRSPSDCFD VAIEAARIAV TYHTPVLILS DGAIANGSEP
WRIPDVGSYA PIAHTFAKSG EPFQPYARDP ETLARQFAVP GTPGLEHRIG GLEAANGSGN
ISYEPKNHDL MVRLRQAKID GIKVPDLEVD DPTGDAELLM VGWGSSYGPI GEACRRARRK
GIKVAHAQLR NLNPFPANLG EVLRRYPKVV LPEMNLGQLA LLLRGKFLVD VQSVTKVEGM
AFLADEIEGI IDAAIDGTLG DKEIEKAKFA RLATATIETG VGANA
//
