ID   A0A1I4G3V2_9PORP        Unreviewed;       651 AA.
AC   A0A1I4G3V2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC {ECO:0000313|EMBL:SFL23741.1};
GN   ORFNames=SAMN05216357_1163 {ECO:0000313|EMBL:SFL23741.1};
OS   Porphyromonadaceae bacterium KH3CP3RA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX   NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFL23741.1, ECO:0000313|Proteomes:UP000198708};
RN   [1] {ECO:0000313|EMBL:SFL23741.1, ECO:0000313|Proteomes:UP000198708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFL23741.1,
RC   ECO:0000313|Proteomes:UP000198708};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOSU01000016; SFL23741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4G3V2; -.
DR   Proteomes; UP000198708; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003869; Polysac_CapD-like.
DR   PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR   PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF02719; Polysacc_synt_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          295..580
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   651 AA;  74160 MW;  F6A6556A30119A0C CRC64;
     MSNLIHNFLS NRVLSRFTIF MIDILMIMFS CLMMYLVRYG FVELTPEVRA DGVTLAIILI
     FVNAVTFILF RTFSGILRFS SFSDLMRITY ALMLGYGFTY LGIIILKRYH PGFYLDDITF
     ISVFFLNTFL MIFSRILTKE VYEFITGRDV KPVNVFIYGT KEAGISVAKA LKGNSEFNYR
     VLGFISDESQ MVGKELMGIT IHANNENIFR TMESKDVKTV IVSPQQMEEI KNADLLSNFV
     DHNISLLTTV PLNEWNGMIM SKEQLKDVQI EDLLPRDPIH INMLKIASNI EGKRIMVTGA
     AGSIGSEIVR QVANFNPYSI ILIDQAETPL HDMRLELKDK WRELRAEIIV ADVSNASRME
     RIFSRTRPQY IFHAAAYKHV PMMEDNVSES VQTNILGTKI VADLAVKYNA DKFVMVSTDK
     AVNPSNVMGC SKRICEIYVQ SLAKYIAKSG KRTTQFITTR FGNVLGSNGS VIPLFREQIK
     NGGPVTVTHP EIIRYFMTIP EACQLVLEAG AMGKGGEIYI FDMGKPVKIL DLAKRMIRLS
     GSKNIKIEFT GLRHGEKLYE ELLNIAEHTK PTYHEKIMIA DVREYEYEEV SRKVDALIHS
     SFEYDDMRTV KKMKEIVPEF RSINSPFEAV DRLLESISEK ETLIPVPKDK G
//