ID A0A0F2RL54_9PROT Unreviewed; 619 AA.
AC A0A0F2RL54;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KJS39318.1};
GN ORFNames=VR70_08405 {ECO:0000313|EMBL:KJS39318.1};
OS Rhodospirillaceae bacterium BRH_c57.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae.
OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS39318.1, ECO:0000313|Proteomes:UP000033468};
RN [1] {ECO:0000313|EMBL:KJS39318.1, ECO:0000313|Proteomes:UP000033468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS39318.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS39318.1}.
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DR EMBL; LAEA01000116; KJS39318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RL54; -.
DR STRING; 1629718.VR70_08405; -.
DR PATRIC; fig|1629718.3.peg.2831; -.
DR Proteomes; UP000033468; Unassembled WGS sequence.
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}.
FT DOMAIN 27..215
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 266..430
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 619 AA; 65414 MW; 870A1D940A14C0A1 CRC64;
MPSSALAAAT ATEALDRVTV RFAGDSGDGM QLTGSIFTES TALASHDLST FPDYPAEIRA
PTGTTYGVSA YQINFGAQGV LTAGDAPDLL VVMNPAALMV NVAALKAGAT IILDSDAFGT
RAIERAGYTT DPRADNSLAP FTVVDLPITS LTQQAAQPLG LSKREAQRCK NVWTLGLVLW
MFDRDRAPII EALRTKFRKA PEIAEANVAV LNAGHAYGET AEIPALRRLP VTRSLPAPGL
YRTVTGAEAT ALGLVAGAEL TGLDMFLGTY PITPASPMLH HLARLRDWGV TTFQAEDEIA
AVCAAIGASY AGKLGVTTSS GPGIALKTEA LGLAISAELP LVVVNAQRGG PSTGLPTKTE
QSDLFQAVMG RNGDAPIPVI AARSPSDSFD AAIEAVKIAV RHMTPVFLLI DGYIGNASEP
WHLPDMDTYE RAPVAFRRPD DGTGAFDRDP ESLGRQWTLP GTPGLEYRIG GLEKDFSTGA
VSYDSANHQR MTDLRSGKMD AIARALPPQE VCEGPTSGKL AVVAWGSTYG PVHRAVVEAN
RMGRAVAHIH LRHIAPFAPN LTDLLAGFDT VLVPEMNTGQ LALLLQAHTL RKVERLNKVT
GQPFKIAEIS AAIESALES
//
