ID   A0A1X7L7H7_9BACT        Unreviewed;       650 AA.
AC   A0A1X7L7H7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC {ECO:0000313|EMBL:SMG49129.1};
GN   ORFNames=SAMN05661096_03565 {ECO:0000313|EMBL:SMG49129.1};
OS   Marivirga sericea.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX   NCBI_TaxID=1028 {ECO:0000313|EMBL:SMG49129.1, ECO:0000313|Proteomes:UP000193804};
RN   [1] {ECO:0000313|EMBL:SMG49129.1, ECO:0000313|Proteomes:UP000193804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4125 {ECO:0000313|EMBL:SMG49129.1,
RC   ECO:0000313|Proteomes:UP000193804};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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DR   EMBL; FXAW01000008; SMG49129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7L7H7; -.
DR   STRING; 1028.SAMN05661096_03565; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000193804; 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   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR   PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF13727; CoA_binding_3; 1.
DR   Pfam; PF02719; Polysacc_synt_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..582
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   650 AA;  73612 MW;  EFEB8C620D564C73 CRC64;
     MIKKINDISF LPRWIILLID LLLLMFAIVV AYFLRFNFNV AEVLAFKFTE GLVLFLICHL
     IAIFLTQSYA GIIRYTSIED GLRISYTTFI GTLLIAIVSY LNYWYTGSVI IPLSVLIISF
     IFSVVILFSY RVLVKNLFAY YRDAVRHRKN VMIFGAGQYG IITKQVIDAD PNARMRVVGF
     VDDDLKKVGK VINGAPIYDA GYNLDAILKK YHIHEIVIAI ANLSVERKNE LVDYCLKAHV
     KVRTVPSPDK WVNGELSMNQ IKEVRIEDLL GRESIKLENP KVSENIGGKT VLITGAAGSI
     GSEIAKQILK VKPKKLILLD QAESFLYAID IELTNLDDNQ EIEIVPVIMD VANKRRLEIV
     FDKYRPDVVY HAAAYKHVPL MEMHPFEAVA TNVYGTKNLA DLSVQYNVKK FVMVSTDKAV
     NPTNVMGATK RLAEIYVQSL NDSNSHDVKN NTQFITTRFG NVLGSNGSVI PLFKKQIEKG
     GPLTVTHPDV TRYFMTIPEA CQLVIEAGIM GFGGEIFVFD MGKSIKIIDL AKKMIRLSGY
     EVDLDIKIVF TGLREGEKLF EELLGDKETT LPTHHEKILI AKTERMAHET IIKELQKLND
     LMNDENELGM IMQMKNILPE FVSHASRFEA LDQELASERK RKWSITRKIS
//