ID A0A098EZP8_9BACI Unreviewed; 577 AA.
AC A0A098EZP8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:CEG26872.1};
GN ORFNames=BN1002_01724 {ECO:0000313|EMBL:CEG26872.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26872.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG26872.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG26872.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCXR01000001; CEG26872.1; -; Genomic_DNA.
DR RefSeq; WP_048824528.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098EZP8; -.
DR STRING; 1476857.BN1002_01724; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000042335; 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:UP000042335}.
FT DOMAIN 14..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 209..449
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 474..562
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 577 AA; 63335 MW; 853BC62A95EB855B CRC64;
MINQLSWKVG GQQGEGIEST GEIFAIALNR LGYYLYGYRH FSSRIKGGHT NNKIRVSTTQ
VRSISDDLDI LVAFDQETID LNYKELHSKG VILADAKFNP QKPADTQAEL YAVPFTEIAT
ELGTSLMKNM VAIGATTAVL DLDIPVFEEV VREIFGRKGD QVVAKNMEAI QAGHDFMTEQ
LAGIRTMQLE KADGKKRLFM IGNDAIALGA LAAGCRFMAA YPITPASEIM EYLIKKLPPL
GGTVIQTEDE IAAATMVIGA NYAGVRAITA SAGPGLSLKM EAIGLAGMTE TPIVIIDTQR
GGPSTGLPTK QEQSDLMQMI YGTHGEIPKI VIAPSTVQEA FYDTAEALNL AEEYQCPVIV
LSDLQLSLGK QTVEPLDFSK IEIRRGKLVT EELPEIDNKG YFKRYEVTED GVSPRVVPGM
KNGIHHVTGV EHDETGKPSE SATNRIAQMD KRFRKVKNLR FKTPVHVNAP HEEADLLIVG
FNSTRGAIEE AISRLSSEGH KVNHAHIRLI HPFPADEVLP LFKSAKKIMV VENNATGQLA
NIIKMNVGHA DKMFNLLKYD GNPFLPNEIY TKSKELF
//
