ID A0A2W2LNQ8_9ACTN Unreviewed; 642 AA.
AC A0A2W2LNQ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:PZH12182.1};
GN ORFNames=C1I97_12590 {ECO:0000313|EMBL:PZH12182.1};
OS Streptomyces sp. NTH33.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1735453 {ECO:0000313|EMBL:PZH12182.1, ECO:0000313|Proteomes:UP000248559};
RN [1] {ECO:0000313|EMBL:PZH12182.1, ECO:0000313|Proteomes:UP000248559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTH33 {ECO:0000313|EMBL:PZH12182.1,
RC ECO:0000313|Proteomes:UP000248559};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Streptomyces sp. NTH33.";
RL Submitted (JAN-2018) 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:PZH12182.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; POTZ01000096; PZH12182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2LNQ8; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000248559; 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:UP000248559}.
FT DOMAIN 44..231
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 286..494
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 541..624
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 68757 MW; 2D6817FFDE24E3FF CRC64;
MTSQVSSPAE QADGAVVGEQ RKAAGTKDVR RLDRVIIRFA GDSGDGMQLT GDRFTSETAS
FGNDLSTLPN FPAEIRAPAG TLPGVSSFQL HFADHDILTP GDAPNVLVAM NPAALKANIG
DLPRGAEIIV NTDEFTKRAM AKVGYDASPL QDGSLDGYHL HPVPLTTLTV EALKEFDLSR
KEAERSKNMF ALGLLSWMYH RPTEGTEKFL RKKFAKKPDI AAANIAAFRA GWNFGETTED
FAVSYEVVPA TKAFPVGTYR NISGNLALAY GLIAASRQAD LPLYLGSYPI TPASDILHEL
SRHKNFGVRT FQAEDEIAGI GAALGAAFGG SLAVTTTSGP GVALKSETIG LAVSLELPLL
VVDIQRGGPS TGLPTKTEQA DLLQAMYGRN GEAPVPVVAP RTPADCFDAA LDAARIALTY
RTPVFLLSDG YLANGSEPWR IPELDELPDL TVQFAQGPNH TLADGTEVFR PYKRDAKTLA
RPWAVPGTPG LEHRIGGIEK QDGTGNISYD PANHDFMVRT RQAKVDGIEV PDVEVDDPTG
ARTLVLGWGS TYGPITAAVR RLRAAGESIA QAHLRHLNPF PKNLGAVLQA YDKVVIPEMN
LGQLATLVRA KYLVDAHSYN QVNGMPFKAE QLATALKEAI DG
//
