ID A0A255T7L6_9BACT Unreviewed; 637 AA.
AC A0A255T7L6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:OYP60845.1};
GN ORFNames=CIL02_07305 {ECO:0000313|EMBL:OYP60845.1};
OS Prevotella sp. P3-122.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP60845.1, ECO:0000313|Proteomes:UP000215645};
RN [1] {ECO:0000313|EMBL:OYP60845.1, ECO:0000313|Proteomes:UP000215645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3-122 {ECO:0000313|EMBL:OYP60845.1,
RC ECO:0000313|Proteomes:UP000215645};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYP60845.1}.
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DR EMBL; NPJH01000038; OYP60845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255T7L6; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000215645; 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:UP000215645}.
FT DOMAIN 22..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 261..443
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 513..578
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 637 AA; 68839 MW; 66D5DF6DE7320878 CRC64;
MTEEIEIKEL SEVVVRFSGD SGDGMQLAGN IFSTISATVG NGISTFPDYP ADIRAPQGSL
TGVSGFQVHI GSGPVYTPGD QCDVLVAMNA AALKTQYKYA KPQATIIIDT DSFGAMDLKK
ADFKTDDYLA ELGIDPDRVV ACPITQMVKA IAADSTDSKT ALKCRNMFAL GLVCWLFNRE
VSLVENFLRE KFARKPQVAE LNIKVVNAGY DYGHNVHASV PATYRIESKT KVPGRYMDIT
GNKATAYGLI AAAEKAGLKL FLGSYPITPA TDILHELSKH KSCGVITVQC EDEISGCASA
VGAAFAGALA ATSTSGPGIC LKSEAINLAV IDELPLVIID VQRGGPSTGL PTKSEQTDLL
QALYGRNGES PMPIIAATSP TDCFDAAYRA AKMALEHMTP VILLTDAFIA NGSAAWKLPK
MDELPDIRPH YVTEEQKYKY TPYVRDPESQ VRYWAIPGQE GYTHILGGLE KDGKTGAIST
EPENHNKMSH IRYQKVARIP VPDMVVEGDA DDAELLIVGF GSTYGHLLSA TNVLRSRGHK
VAMAQVKFVN PLPANIAEVL MRYPKVVVAE QNLGQLAALL RIRVNGFAPY QYNQVKGQPF
VVNDLVEEFE RLLETKAVPS GAQTFDTKVL NAPNINI
//
