ID W0ETP8_9BACT Unreviewed; 615 AA.
AC W0ETP8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:AHF12496.1};
GN ORFNames=BARVI_06625 {ECO:0000313|EMBL:AHF12496.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF12496.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF12496.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007034; AHF12496.1; -; Genomic_DNA.
DR RefSeq; WP_025278440.1; NZ_CP007034.1.
DR AlphaFoldDB; W0ETP8; -.
DR STRING; 880074.BARVI_06625; -.
DR KEGG; bvs:BARVI_06625; -.
DR PATRIC; fig|880074.11.peg.1384; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_10; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000018901; 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; 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; 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}.
FT DOMAIN 22..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 260..434
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 615 AA; 66681 MW; 715A2898ED80B17A CRC64;
MTEKTNVKVL EEVVVRFSGD SGDGMQLAGN IFSNVSAGVG DEISTFPDYP AEIRAPQGTL
GGVSGFQVHI GRGVHTPGDL ADVLVAMNPA ALKTNARHVK RGGVVIIDSD SFRASDLEKA
AFKTDDPIQE AGLSHAQIVP VPITQMVKDS LADSGLDNKS IVRCKNMFAL GLVCWLFDRP
LEQAQHLLKN KFAKKLAIYE ANAKVMNDGY NYGHNIHASV STYRVESAQV RPGIYTDVNG
NTATAWGLIA ASEKSGLPLF LGSYPITPAT DILHELAKRK DLGVKAIQVE DEIAGVCTAI
GASFAGNLAV TSTSGPGLAL KSEGIGLAVM SELPLVVIDV QRGGPSTGLP TKTEQTDLLQ
ALYGRNGESP VVVLAASTPT NCFDMAFRAA KIALEHMTPV ILLTDGFIGN GSSAWRIPDM
DEYPDIKPNY VKPEQLGVWK PYDRDERSVR YWARPGLEGF MHRLGGLEKD SKTSAISTDP
VNHEKMVRAR QQKIDNIAND LPLLNVQGNP DADLLVVGWG GTYGHLYSAV EALNAQGKPV
AFVHFNYINP LPLNTEEIIR RYKRVVVCEL NNGQFAAYLS GKVPGKTFLR YNKIQAQPFM
VSELIEHFTK LLEEE
//
