ID Q732V1_BACC1 Unreviewed; 585 AA.
AC Q732V1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase, alpha subunit, putative {ECO:0000313|EMBL:AAS42714.1};
GN OrderedLocusNames=BCE_3809 {ECO:0000313|EMBL:AAS42714.1};
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS42714.1, ECO:0000313|Proteomes:UP000002527};
RN [1] {ECO:0000313|EMBL:AAS42714.1, ECO:0000313|Proteomes:UP000002527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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DR EMBL; AE017194; AAS42714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q732V1; -.
DR KEGG; bca:BCE_3809; -.
DR HOGENOM; CLU_017038_1_0_9; -.
DR Proteomes; UP000002527; 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 Pyruvate {ECO:0000313|EMBL:AAS42714.1}.
FT DOMAIN 14..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..448
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 476..571
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 585 AA; 64474 MW; DF558D0D0A34B42A CRC64;
MISQLSWKVG GQQGEGIEST GEIFCIALNR LGYYLYGYRH FSSRIKGGHT NNKIRVSTTE
VRAISDDLDI LIAFDQETID FNFHELRPGG IVVADAKFNP TIPDNTDVNL YVIPFTDIAS
ELGTSLMKNM VAVGASSAVL GLDETAYLDV VEEIFGRKGE QVVQKNMDAI KRGSQYMKEL
LGEKVNMMQL EKADGQKRMF MIGNDAIAFG AVAGGARFMS AYPITPASEI MEYLIKKLPK
VGGTVIQTED EIAACTMAIG ANYAGVRTLT ASAGPGLSLM MEAIGLAGIT ETPLVIVDTQ
RGGPSTGLPT KQEQSDLMAM IYGTHGEIPK IVMAPSTVEE AFYDIVEAFN LSEEYQVPVI
FLTDLQLSLG KQTVEPLKLD KVEIRRGKLD LEAELPEREN KAYFKRYEVT EDGVSPRVLP
GMKNGVHHVT GVEHDETGKP SESAINRKDQ MDKRFRKMEN LKFNTPVYKN VKHEEADVLL
VGFNSTRGAI EEAMERLEQE GMKVNHAHVR LIHPFPTAEI DPLVKNAKRV VVVENNATGQ
LANIMKMNLG NGEKISSLLK YDGNPFLPKE IYNECKKGVV LNGNI
//
