ID B9KDD9_CAMLR Unreviewed; 587 AA.
AC B9KDD9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=UDP-N-acetylglucosamine C-6 dehydratase {ECO:0000313|EMBL:ACM64578.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:ACM64578.1};
GN Name=pglF {ECO:0000313|EMBL:ACM64578.1};
GN OrderedLocusNames=Cla_1258 {ECO:0000313|EMBL:ACM64578.1};
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM64578.1, ECO:0000313|Proteomes:UP000007727};
RN [1] {ECO:0000313|EMBL:ACM64578.1, ECO:0000313|Proteomes:UP000007727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060
RC {ECO:0000313|Proteomes:UP000007727};
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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DR EMBL; CP000932; ACM64578.1; -; Genomic_DNA.
DR RefSeq; WP_012661961.1; NC_012039.1.
DR AlphaFoldDB; B9KDD9; -.
DR STRING; 306263.Cla_1258; -.
DR GeneID; 7410991; -.
DR KEGG; cla:CLA_1258; -.
DR PATRIC; fig|306263.5.peg.1245; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_5_2_7; -.
DR Proteomes; UP000007727; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; 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; 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 Lyase {ECO:0000313|EMBL:ACM64578.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..546
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 587 AA; 66345 MW; 28E2DBF63221707B CRC64;
MDYKSKRLGF FLGADILLFV ISIYLSFSLR FSADIPSEFY EGMFKSAVVL IALKIIFLAI
FRIYQVAWRF FSLNEARKLV IALALAELVF LAIYYFYDDF FNPFPRSVIG IDFVLSCMLI
GSLRISKRMV VDFRKPKYNE EHPCIVVGAT SKALHLLKGA KEGSLGLFPV AVVDERKNLI
GTYCDKFIVE EKEAIKKYTQ EGIHTAIIAL KLEQEELKKL FDELISYGIN DIKLFSFTQN
EARDISIEDL LARKPKDLDN ACVIDFIKDK VVLVSGAGGT IGSELCKQCI KFGAKHLIML
DHSEYNLYKI SEDLNQHKEK IEAIMMSILD KEALEKLLSS KKIDLILHAA AYKHVPLCEQ
NPHSAILNNI IGTKNLIDLA KTYKVAKFVM ISTDKAVRPT NIMGCTKRIC ELYTLSSSCE
NFEVACVRFG NVLGSSGSVI PKFKAQIAAN EPLTLTHPDI VRYFMLVDEA VQLVLQAAAI
AKGGELFVLD MGEPVKIMDL AKKMLLLSNK KLEIKITGLR KGEKLYEELL IHEDDLKTQY
ESIFVTTSEI KDLKILNQEI ERLLQSTDPT KVLKEIVPEF NHNKNGE
//
