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Database: UniProt
Entry: A0A432WD66_9GAMM
LinkDB: A0A432WD66_9GAMM
Original site: A0A432WD66_9GAMM 
ID   A0A432WD66_9GAMM        Unreviewed;       647 AA.
AC   A0A432WD66;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Nucleoside-diphosphate sugar epimerase {ECO:0000313|EMBL:RUO30345.1};
GN   ORFNames=CWE14_13325 {ECO:0000313|EMBL:RUO30345.1};
OS   Aliidiomarina soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=1928574 {ECO:0000313|EMBL:RUO30345.1, ECO:0000313|Proteomes:UP000287823};
RN   [1] {ECO:0000313|EMBL:RUO30345.1, ECO:0000313|Proteomes:UP000287823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4G10-17 {ECO:0000313|EMBL:RUO30345.1,
RC   ECO:0000313|Proteomes:UP000287823};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO30345.1}.
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DR   EMBL; PIPO01000006; RUO30345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432WD66; -.
DR   Proteomes; UP000287823; 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   Reference proteome {ECO:0000313|Proteomes:UP000287823};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          281..592
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   647 AA;  71603 MW;  10414A73CF21FB7B CRC64;
     MIRRLFSLPR ETKRVVSLVI DVLALLFAYL FALSVRYETW YLPPDADVWG AIIIAIVVSL
     GLFAKFGLYR AVVRYMALSA LMTVFFGVVS SSVVLALAVY VLGASVPPSV IVNYTLMSLV
     LIGGLRLLMR ALYEQHANKR KERVIIYGAG SAGRQLAQAI SNGAEYHPVC FVDDDTTLHG
     STMLGLRVRS PNELAHCIDE CEAGRVLLAM PRISRARRKQ ILDFLEPLKV QVQTVPGMAD
     MVDGNVSIDD LQDVNIEDLL GRDPVQPRQA LMNTNIRGKR VLVTGAGGSI GAELCRQIIR
     CEPETLVLAE VSEFNLYRIE RELSQAIAEG QLMVQLRPAL CSVQDRKRLT ELMQIFKIDT
     VYHAAAYKHV PIVEYNIVEG VRNNVFGTWN AAEAAATAGV SDFVLISTDK AVRPTNVMGA
     TKRMSELVLQ ALAKREESKR DQQLEGNHVT FSMVRFGNVL GSSGSVVPLF REQIINGGPV
     TVTDPEITRY FMTIPEAAQL VIQAGAMGSL TARELKNNGG SVFVLDMGEP VKIDYLARKL
     IRLMGLEVKD QNNPEGDIEI TYSGLRPGEK LYEELLIGDN VQPTDHPRIM TACEADLPWA
     DVKEILELLD SYCHTLKIRD IHDLLQRVPL GFTPSSGIND LLWLAQD
//
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