PGLF_CAMJE
ID PGLF_CAMJE Reviewed; 590 AA.
AC Q0P9D4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase;
DE Short=UDP-GlcNAc C6 dehydratase;
DE EC=4.2.1.135;
DE AltName: Full=Protein glycosylation pathway protein F;
DE AltName: Full=UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining);
GN Name=pglF; OrderedLocusNames=Cj1120c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16286454; DOI=10.1074/jbc.m511021200;
RA Schoenhofen I.C., McNally D.J., Vinogradov E., Whitfield D., Young N.M.,
RA Dick S., Wakarchuk W.W., Brisson J.R., Logan S.M.;
RT "Functional characterization of dehydratase/aminotransferase pairs from
RT Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid
RT and bacillosamine biosynthetic pathways.";
RL J. Biol. Chem. 281:723-732(2006).
CC -!- FUNCTION: C6 dehydratase involved in the bacillosamine biosynthesis
CC pathway by generating UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-
CC hexulose from UDP-N-acetyl-alpha-D-glucosamine. Involved in the N-
CC linked protein glycosylation pathway. {ECO:0000269|PubMed:16286454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-
CC dideoxy-alpha-D-xylo-hex-4-ulose; Xref=Rhea:RHEA:30823,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57705, ChEBI:CHEBI:62375;
CC EC=4.2.1.135; Evidence={ECO:0000269|PubMed:16286454};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL35237.1; -; Genomic_DNA.
DR PIR; C81316; C81316.
DR RefSeq; WP_002858054.1; NC_002163.1.
DR RefSeq; YP_002344513.1; NC_002163.1.
DR AlphaFoldDB; Q0P9D4; -.
DR SMR; Q0P9D4; -.
DR IntAct; Q0P9D4; 1.
DR STRING; 192222.Cj1120c; -.
DR PaxDb; Q0P9D4; -.
DR PRIDE; Q0P9D4; -.
DR EnsemblBacteria; CAL35237; CAL35237; Cj1120c.
DR GeneID; 905411; -.
DR KEGG; cje:Cj1120c; -.
DR PATRIC; fig|192222.6.peg.1102; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_5_2_7; -.
DR OMA; HVPLCEL; -.
DR BioCyc; MetaCyc:MON-17318; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..590
FT /note="UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase"
FT /id="PRO_5000075135"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 397
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 303..308
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 329..330
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 393..394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 434..438
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 590 AA; 66766 MW; 72A43C7B446C07E0 CRC64;
MIFYKSKRLA FFLTSDIVLI LLSVYLAFSL RFSGDIPSIF YHGMMVSAII LLVLKLSFLF
VFRIYKVAWR FFSLNEARKI FIALLLAEFC FFLIFYFFSD FFNPFPRSAI VIDFVLSYMF
IGTLRISKRM LVDFKPSRMK EEETPCIVVG ATSKALHLLK GAKEGSLGLF PVGVVDARKE
LIGTYCDKFI VEEKEKIKSY VEQGVKTAII ALRLEQEELK KLFEELVAYG ICDVKIFSFT
RNEARDISIE DLLARKPKDL DDSAVAAFLK DKVVLVSGAG GTIGSELCKQ CIKFGAKHLI
MVDHSEYNLY KINDDLNLYK EKITPILLSI LDKQSLDEVL KTYKPELILH AAAYKHVPLC
EQNPHSAVIN NILGTKILCD SAKENKVAKF VMISTDKAVR PTNIMGCTKR VCELYTLSMS
DENFEVACVR FGNVLGSSGS VIPKFKAQIA NNEPLTLTHP DIVRYFMLVA EAVQLVLQAG
AIAKGGELFV LDMGKPVKII DLAKKMLLLS NRNDLEIKIT GLRKGEKLYE ELLIDENDAK
TQYESIFVAK NEKVDLDWLN KEIENLQICE DISEALLKIV PEFKHNKEGV
