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Database: UniProt
Entry: A0A0F6A264_9GAMM
LinkDB: A0A0F6A264_9GAMM
Original site: A0A0F6A264_9GAMM 
ID   A0A0F6A264_9GAMM        Unreviewed;       621 AA.
AC   A0A0F6A264;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Nucleoside-diphosphate sugar epimerase {ECO:0000313|EMBL:KKD61330.1};
GN   ORFNames=RN22_06320 {ECO:0000313|EMBL:KKD61330.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD61330.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD61330.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD61330.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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:KKD61330.1}.
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DR   EMBL; LASY01000026; KKD61330.1; -; Genomic_DNA.
DR   RefSeq; WP_046303574.1; NZ_LASY01000026.1.
DR   AlphaFoldDB; A0A0F6A264; -.
DR   PATRIC; fig|1581149.3.peg.1816; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..578
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   621 AA;  68934 MW;  517C5E44A1A0A3EE CRC64;
     MFTPIQLLLS AQRRNKRIIS IIYDLLAVIF SFYFAMALRL DSVHIPFGFK EALCLAVTGS
     VTVFCFIKLG MYRAILRYMM MPAVGNIFIA VVLSSITLAL SGFFLQAFIP RSVPFIYAGI
     AMIMLGAPRI IIRTVYYHYY RRQKPNVFIY GAGSTGRDLA YALIQGDEYH PVVFLDDDPK
     KVGQIITGVR VYPADEFDRL MSLYEPVKLL LAINNINKGE RLRLLDKLSN WPIEVQSVPS
     VEDIASGKAL ATEIRDLEIE DLLGREPVKP DLKLMSKNIT GKNILVTGAG GSIGSELCRQ
     ILTQQPARLV LVELNEYNLY TIHHELVETA KSLNLTVDIV AALGSVQKEN RMTKLMENNC
     IHTVYHSAAY KHVPLVEDNI IEGIRNNVFG SLHCANAAIA AGVESFTLIS TDKAVRPTNI
     MGASKRMAEL ILQALAEKGT STCFTMVRFG NVLGSSGSVV PLFKKQIRNG GPVTVTHPDI
     IRYFMLIPEA AQLVIQASAM GHNGQVFVLD MGEAVKIHDL ALRMIHLMGM KEYVVGSGEE
     GDIEIKFTGL RPGEKLFEEL LIGDNVEGTG HQKIMTAREE SLSWSEMAEI IEKLDECCHD
     FNIACIKRIL LDAPTGYKPE V
//
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