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Database: UniProt
Entry: S7WT64_9BACT
LinkDB: S7WT64_9BACT
Original site: S7WT64_9BACT 
ID   S7WT64_9BACT            Unreviewed;       423 AA.
AC   S7WT64;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=UDP-N-acetylglucosamine 4,6-dehydratase {ECO:0000313|EMBL:EPR69949.1};
DE            EC=4.2.1.- {ECO:0000313|EMBL:EPR69949.1};
GN   ORFNames=ADICYQ_1145 {ECO:0000313|EMBL:EPR69949.1};
OS   Cyclobacterium qasimii M12-11B.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR69949.1, ECO:0000313|Proteomes:UP000014974};
RN   [1] {ECO:0000313|EMBL:EPR69949.1, ECO:0000313|Proteomes:UP000014974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12-11B {ECO:0000313|EMBL:EPR69949.1,
RC   ECO:0000313|Proteomes:UP000014974};
RX   PubMed=23950138;
RA   Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT   from Arctic Marine Sediment.";
RL   Genome Announc. 1:e00642-13(2013).
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:EPR69949.1}.
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DR   EMBL; ATNM01000052; EPR69949.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7WT64; -.
DR   STRING; 641524.ADICYQ_1145; -.
DR   PATRIC; fig|641524.5.peg.1138; -.
DR   eggNOG; COG1086; Bacteria.
DR   Proteomes; UP000014974; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:EPR69949.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          305..415
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   423 AA;  47979 MW;  2F3F33CC71E86C51 CRC64;
     MEKVLNSKLN PLKNFLKNDK HIHPLLILSV DIFIVFISFT FAFLIIGGFG FDQMEFVQYI
     LATGCFCAIA LPVIYFSKLH TGLLRYSNST DLFHIFIAAL GFSLLFVGFY YGIGHRWISL
     NSSFLMLVLL VNFFIVSTLL IAFRLLAKAT FLVLISKMSN RSVHRVLIFG SDQNAVLVKQ
     ALSNDPNINY IVEGFISTDR SMLNNYLVQK KVYHIKELSR LKKQKDIQEL LITNENLNGR
     DKRVVIERCI RLGIKVFTIP PAKNWLSGEL PSKQIKKLRI EDLLQRKPIV IDQSKVKSDL
     EGKKVLVTGA AGSIGSEIVR QVLSYKPSLL IMCDHAESPL HEIQLSMEDE FPGAKMEVVL
     ADVSNYERMH KLFNICRPQI VYHAAAYKHV PMIENNPFEA ISVNVGGTRN IADLSVFLRL
     ISL
//
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