ID W8T8B9_PEPAC Unreviewed; 563 AA.
AC W8T8B9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=2-oxoglutarate synthase subunit KorA {ECO:0000313|EMBL:AHM57954.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:AHM57954.1};
GN Name=korA {ECO:0000313|EMBL:AHM57954.1};
GN ORFNames=EAL2_808p04510 {ECO:0000313|EMBL:AHM57954.1};
OS Peptoclostridium acidaminophilum DSM 3953.
OG Plasmid EAL2_808p {ECO:0000313|EMBL:AHM57954.1,
OG ECO:0000313|Proteomes:UP000019591}.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM57954.1, ECO:0000313|Proteomes:UP000019591};
RN [1] {ECO:0000313|EMBL:AHM57954.1, ECO:0000313|Proteomes:UP000019591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM57954.1,
RC ECO:0000313|Proteomes:UP000019591};
RC PLASMID=Plasmid EAL2_808p {ECO:0000313|Proteomes:UP000019591};
RX PubMed=24926057;
RA Poehlein A., Andreesen J.R., Daniel R.;
RT "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT acidaminophilum al-2 (DSM 3953).";
RL Genome Announc. 2:e00573-14(2014).
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DR EMBL; CP007453; AHM57954.1; -; Genomic_DNA.
DR RefSeq; WP_025436804.1; NZ_CP007453.1.
DR AlphaFoldDB; W8T8B9; -.
DR KEGG; eac:EAL2_808p04510; -.
DR PATRIC; fig|1286171.3.peg.2630; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000019591; Plasmid EAL2_808p.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AHM57954.1}; Plasmid {ECO:0000313|EMBL:AHM57954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019591}.
FT DOMAIN 12..165
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 194..433
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 458..551
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 563 AA; 61887 MW; 714159FC323FAC29 CRC64;
MQNFNILIGG SAGQGIDTLS SSIEKTLHKM GYYIFSNKDY ESRVRGGHNF TQVRFGNLPV
YSHSESLDMI IALNEEAIEV HKDKLSEGGI ILCDESITSA GDKFVPRPLN RTAKQIGNAM
VANTVAFGAV CKLIGLDIEI AKDMINASFG EEYAGGNLMA FDEGYGMLQR RFNLEEPSAK
NQMLINSNQA IALGALAGGV MFYAAYPMTP STGILTYLAA KTMETDLIVE QAEDEIAAIQ
MALGASYAGV RAMTGTSGGG FALMVEALSL AGMIETPIVI VDSQRPGPAT GFPTRTEQGD
LSFVLNAGHG EFSRMVIAVR SPEDAFYQTV RALNLADEFQ IPVIILTDQH LADSNQTADK
FDMSRVKIER HISDFTVLAE YGDYGRYRLT ETGLSPRIIP GKNENQTVLV DSDEHDELGH
IVEDANTRIK MVNKRLGKME LLKQKVKEPD YYGTDSPEVL LIGWGSTEGA LREAVEILNG
RGERFGTLVF GDIWPLPIQM LEKYSENAKI VVNVEQNATG QLGRLIRQET GILIERSILK
YDGRQINAEE IVRRFNEENA IVR
//
