ID A0A135L4T9_9BACI Unreviewed; 581 AA.
AC A0A135L4T9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0008006|Google:ProtNLM};
GN ORFNames=U473_08400 {ECO:0000313|EMBL:KXG44024.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG44024.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG44024.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG44024.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-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:KXG44024.1}.
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DR EMBL; LSKU01000001; KXG44024.1; -; Genomic_DNA.
DR RefSeq; WP_068725247.1; NZ_LSKU01000001.1.
DR AlphaFoldDB; A0A135L4T9; -.
DR STRING; 1413211.U473_08400; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000070352; 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; 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:UP000070352}.
FT DOMAIN 14..173
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 211..451
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 475..568
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 416..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 63692 MW; 5DD2530E4A21A49F CRC64;
MRNEVVWKVG GQQGEGIDST GEIFALALAR KGYFISSNKH FASRIKGGYT HYQIRVTTEP
AYYHGDYTDV LLALDQETID NNLEVMSEGS IILRDGKEET VEKNNHITTF ILPLTQMAEE
IGGKIVRNMV SLGASAALFG LDEDLFDSLI EDKFSKKGEE IISMNKNAVR AGHKKAKEFI
KAGKLSVIQL EKPEQQISRS LMIGNAAVGF GALAGGCRFL SAYPITPASE VMEWLKKELP
RVGGTVVQAE DEIAGITMAI GAAYSGVRAM TSTSGPGFSL KTEALGLAGI SETPLVIMNT
QRGGPGTGLP TKYEQADLNT MINAGHGEIP RIVLAPSTVE EAFYMTAQAF NYAEEYQCPV
ILAMDLYLSL FNQTVNKLDF SKIQINRGKL LSDEEVAQNE DRYFLRYEVT EDGISNRSIP
GQKGGVHTAN SNEHNQTGHI DEDTTNRVNM MKKRLGKLAT LTDQGFSVDG TKDSDLLIIG
FGSTFGVLQE AKKSLEKQGL KVTHTHIKRL TPFDTSLTDY ILAAKKVVVI ENNYTGQLKR
LIQMECNTGK ELGSIVKYDG NPFTLKEVVD QINAIMAKEV K
//
