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
//