ID J1RDR1_9NOCA Unreviewed; 642 AA.
AC J1RDR1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein {ECO:0000313|EMBL:EJJ02419.1};
GN ORFNames=JVH1_0198 {ECO:0000313|EMBL:EJJ02419.1};
OS Rhodococcus sp. JVH1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=745408 {ECO:0000313|EMBL:EJJ02419.1, ECO:0000313|Proteomes:UP000009024};
RN [1] {ECO:0000313|EMBL:EJJ02419.1, ECO:0000313|Proteomes:UP000009024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JVH1 {ECO:0000313|EMBL:EJJ02419.1,
RC ECO:0000313|Proteomes:UP000009024};
RX PubMed=22965106; DOI=10.1128/JB.01066-12;
RA Brooks S.L., Van Hamme J.D.;
RT "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL J. Bacteriol. 194:5492-5493(2012).
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:EJJ02419.1}.
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DR EMBL; AKKP01000001; EJJ02419.1; -; Genomic_DNA.
DR RefSeq; WP_009472466.1; NZ_AKKP01000001.1.
DR AlphaFoldDB; J1RDR1; -.
DR PATRIC; fig|745408.3.peg.187; -.
DR Proteomes; UP000009024; 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 Pyruvate {ECO:0000313|EMBL:EJJ02419.1}.
FT DOMAIN 27..214
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 265..480
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 521..606
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 642 AA; 67334 MW; BB271632BFC0B045 CRC64;
MESTTQSATG PVTKLEQVVI RIAGDSGDGM QLAGDQFTAE AAAFGNDLAT QPNFPAEIRA
PQGTLPGVSS FQIQIAEYDI LTAGDRPDVL VAMNPAALKA NIGDLPRGGT LIVNSDEFTK
RNLSKVGYDG DPLETAEFED YQIHEIAMAT LTLGAVESVG LGKKDAERSK NMFALGVLSW
MYGRPLAAIE EFLGSKFAKK PDIAKANVLA LRAGWNYGET TESFATSFEV APATLPAGTY
RQVTGNTALA YGLLAAGRTS GMDVFLGTYP ITPASDILHE LSKHKHFGVV TFQAEDEISG
IGAALGASYG GALGVTSTSG PGLALKSEAI GLAVMTELPL VIVDVQRGGP STGLPTKTEQ
SDLLQALYGR NGESPVAVIA PQSPADCFDA ALEAARIAVT YRTPVLVLSD GAIANGSEPW
SIPDVGALPP IDPAFAVTGH GGGADGGYLP YARDPQTLAR DWAVPGSAGL EHRIGGLEKE
NGSGDISYTD VNHELMTRIR AAKIAGIEVP DLIVDDPDGD ADVLVIGWGS SYGPIGEAVR
RMRRGGNKIA RAHLRHLNPM PANLAEVLTG YRRVLAPEMN LGQLSMLLRA RFDADIQPVT
KVSGMAFRAD ELHEAFLQEF GGTLAASESA KTPAARAAVV TR
//
