PGLE_CAMJE
ID PGLE_CAMJE Reviewed; 386 AA.
AC Q0P9D3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=UDP-N-acetylbacillosamine transaminase;
DE EC=2.6.1.34;
DE AltName: Full=Protein glycosylation pathway protein E;
DE AltName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase;
DE AltName: Full=UDP-4-keto-6-deoxy-GlcNAc C4 aminotransferase;
GN Name=pglE; OrderedLocusNames=Cj1121c;
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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-131 AND GLU-158.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16690622; DOI=10.1074/jbc.m511714200;
RA Vijayakumar S., Merkx-Jacques A., Ratnayake D.B., Gryski I., Obhi R.K.,
RA Houle S., Dozois C.M., Creuzenet C.;
RT "Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential
RT for protein glycosylation and virulence in Campylobacter jejuni.";
RL J. Biol. Chem. 281:27733-27743(2006).
CC -!- FUNCTION: Aminotransferase involved in the bacillosamine biosynthesis
CC pathway by producing UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-
CC acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose), a precursor
CC used in the production of the glycan component 2,4-diacetamido-2,4,6-
CC trideoxy-alpha-D-glucopyranose. Required for host colonization and
CC virulence. Involved in the N-linked protein glycosylation pathway.
CC {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16690622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + UDP-N-acetylbacillosamine = L-glutamate +
CC UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose;
CC Xref=Rhea:RHEA:31663, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:62375, ChEBI:CHEBI:63277; EC=2.6.1.34;
CC Evidence={ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16690622};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:16690622};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.048 mM for UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-
CC glucosamine {ECO:0000269|PubMed:16286454,
CC ECO:0000269|PubMed:16690622};
CC KM=0.61 mM for UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine
CC {ECO:0000269|PubMed:16286454, ECO:0000269|PubMed:16690622};
CC Note=kcat is 144 min(-1) (PubMed:16286454). kcat is 14.9 min(-1)
CC (PubMed:16690622). {ECO:0000269|PubMed:16286454,
CC ECO:0000269|PubMed:16690622};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- DISRUPTION PHENOTYPE: Cells are impaired for flagella-mediated
CC motility, for invasion of intestinal epithelial cells and for
CC persistence in the chicken intestine. {ECO:0000269|PubMed:16690622}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35238.1; -; Genomic_DNA.
DR PIR; D81316; D81316.
DR RefSeq; WP_002852877.1; NC_002163.1.
DR RefSeq; YP_002344514.1; NC_002163.1.
DR PDB; 4ZTC; X-ray; 2.00 A; A=1-386.
DR PDBsum; 4ZTC; -.
DR AlphaFoldDB; Q0P9D3; -.
DR SMR; Q0P9D3; -.
DR IntAct; Q0P9D3; 2.
DR STRING; 192222.Cj1121c; -.
DR PaxDb; Q0P9D3; -.
DR PRIDE; Q0P9D3; -.
DR EnsemblBacteria; CAL35238; CAL35238; Cj1121c.
DR GeneID; 905412; -.
DR KEGG; cje:Cj1121c; -.
DR PATRIC; fig|192222.6.peg.1103; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_7; -.
DR OMA; RFWATQA; -.
DR BioCyc; MetaCyc:MON-17319; -.
DR BRENDA; 2.6.1.34; 13746.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0047302; F:UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..386
FT /note="UDP-N-acetylbacillosamine transaminase"
FT /id="PRO_0000418960"
FT BINDING 25..28
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 131
FT /note="L->F: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:16690622"
FT MUTAGEN 158
FT /note="E->H: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:16690622"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 245..263
FT /evidence="ECO:0007829|PDB:4ZTC"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:4ZTC"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4ZTC"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:4ZTC"
SQ SEQUENCE 386 AA; 43654 MW; 61F5C4488DE2BB27 CRC64;
MRFFLSPPHM GGNELKYIEE VFKSNYIAPL GEFVNRFEQS VKAYSKSENA LALNSATAAL
HLALRVAGVK QDDIVLASSF TFIASVAPIC YLKAKPVFID CDETYNIDVD LLKLAIKECE
KKPKALILTH LYGNAAKMDE IVEICKENEI VLIEDAAEAL GSFYKNKALG TFGEFGAYSY
NGNKIITTSG GGMLIGKNKE KIEKARFYST QARENCLHYE HLDYGYNYRL SNVLGAIGVA
QMEVLEQRVL KKREIYEWYK EFLGECFSFL DELENSRSNR WLSTALIDFD KNELNSCQKD
INISQKNITL HPKISKLIED LKNEQIETRP LWKAMHAQEV FKGAKAYLNG NSELFFQKGI
CLPSGTAMSK DDVYEISKLI LKSIKA
