ID A0A2T0BCE3_9CLOT Unreviewed; 558 AA.
AC A0A2T0BCE3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=2-oxoglutarate oxidoreductase subunit KorA {ECO:0000313|EMBL:PRR81477.1};
DE EC=1.2.-.- {ECO:0000313|EMBL:PRR81477.1};
GN Name=korA {ECO:0000313|EMBL:PRR81477.1};
GN ORFNames=CLVI_25040 {ECO:0000313|EMBL:PRR81477.1};
OS Clostridium vincentii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR81477.1, ECO:0000313|Proteomes:UP000239471};
RN [1] {ECO:0000313|EMBL:PRR81477.1, ECO:0000313|Proteomes:UP000239471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR81477.1,
RC ECO:0000313|Proteomes:UP000239471};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium vincentii DSM 10228.";
RL Submitted (MAR-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:PRR81477.1}.
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DR EMBL; PVXQ01000029; PRR81477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BCE3; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000239471; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PRR81477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239471}.
FT DOMAIN 11..164
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 193..426
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 456..549
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT COILED 214..241
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 558 AA; 61586 MW; 360AA18319D41EB2 CRC64;
MIYNLLIGGT AGQGMETLAS ILEKLLKRKG FETFTIQDYM SRVRGGHNFF QIRFGNEEIN
SHCNAIDGII ALNTETIQLH IEALKDTGFI ISDDEIDYKD ARVYKLPLKS LAKSIGNPKV
FGSIALGALL KLFNQDLSFV YDLLAETFKE KISSQNLTAF ETGLKEVSVK YDIQSMGKNS
NILINGNDAI ALGALASGCK FYSAYPMTPS TSIMNYLSSK IEEAEIVVEQ AEDEIAAINM
AIGASYTGVR SMTGTSGGGF ALMVEAVGLS SMLEVPLVIA EIQRPGPVTG LPTRTEQADL
KFVIAATPGE VPKMVISLRD PEDAFYQTMR AFNLADKYQI PVILLGDQFL ADSIRTVKPF
DFAKVKIERH LNDEDFAGDK EYKRYSLTKT GISPRIIPGR TPGKTVLVDS DEHDESGHIT
ESSAVRIAMN DKRLRKINYL KEELLEPEYL GEATFDTLLI GWGSLYSPIK EAVNILNSSG
KTKYGALVFG DVWPFPDKLL IDKASKATKI INIEQNATGQ LAQLIRENTG IEIKNNILRY
DGRPLCAEDI INKLREVK
//
