ID C0ZF08_BREBN Unreviewed; 592 AA.
AC C0ZF08;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=2-oxo acid oxidoreductase alpha subunit {ECO:0000313|EMBL:BAH44367.1};
GN OrderedLocusNames=BBR47_33900 {ECO:0000313|EMBL:BAH44367.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH44367.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH44367.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP008955; BAH44367.1; -; Genomic_DNA.
DR RefSeq; WP_015891674.1; NC_012491.1.
DR AlphaFoldDB; C0ZF08; -.
DR STRING; 358681.BBR47_33900; -.
DR KEGG; bbe:BBR47_33900; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_9; -.
DR Proteomes; UP000001877; Chromosome.
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:UP000001877}.
FT DOMAIN 14..176
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 211..452
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 479..574
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 592 AA; 64926 MW; C4854C4FF350FEF7 CRC64;
MISQLSWKVG GQQGEGIEST GEIFSMAMNR MGYHLYSYRH FSSRIKGGHT NNKIRVSTTP
MRAISDDLDI LVAFDQETID FNAHELREGG IIIADAKFNP KLPDGLKPVR FFTVPLTEIA
DELGTSLMKN MVSIGASSAI LGIAVESFRP IVEDMFLRKG EKVVEKNMDA IRRGFDFVNE
LTGGQLPEFQ MEKADPQKQL FLIGNDAIAL GAVAAGCRFM PAYPITPASE VMEYLIKKLP
KLGGTVIQTE DEIAAITMAI GANFAGARSL TASAGPGLSL MMEAIGLAGI TEQPVVIVNT
QRGGPSTGMP TKIEQSDVNA MIYGTHGDIP KVVIAPSTVE ECFYDAVEAF NIAEEYQLPV
ILMTDLTLSL GKQTVVPFDY NKVEIRRGKL LAGQELPEKE QNDLFKRYEV TEDGVSPRVI
PGQKYGLHHV TGVEHDQTGR PSENAANRIQ QMDKRMRKME GVLKNFKGAV TADAPHADAD
VLVVGINSTI GTIQEAKGRL EQEGIKVNHA QIRLLHPFPT EEIKALVDKA KKVVVVEHNA
QAQVTSLLKQ HVGNAEKIES VLKYDGNPFL PKEIYAEVKE LVKHGDYERV SK
//
