PSEG_CAMJE
ID PSEG_CAMJE Reviewed; 274 AA.
AC Q0P8U5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase;
DE EC=3.6.1.57;
DE AltName: Full=Pseudaminic acid biosynthesis protein G;
GN Name=pseG; OrderedLocusNames=Cj1312;
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=16728396; DOI=10.1074/jbc.m602972200;
RA Liu F., Tanner M.E.;
RT "PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked
RT glycosyltransferase.";
RL J. Biol. Chem. 281:20902-20909(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP URIDINE-5'-DIPHOSPHATE, ACTIVE SITE, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF HIS-17; TYR-78 AND ASN-255.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=19483088; DOI=10.1074/jbc.m109.012351;
RA Rangarajan E.S., Proteau A., Cui Q., Logan S.M., Potetinova Z.,
RA Whitfield D., Purisima E.O., Cygler M., Matte A., Sulea T.,
RA Schoenhofen I.C.;
RT "Structural and functional analysis of Campylobacter jejuni PseG: a udp-
RT sugar hydrolase from the pseudaminic acid biosynthetic pathway.";
RL J. Biol. Chem. 284:20989-21000(2009).
CC -!- FUNCTION: Nucleotide sugar hydrolase that catalyzes the fourth step in
CC the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is
CC used to modify flagellin. Mediates the removal of UDP from C-1 of UDP-
CC 2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose forming 2,4-
CC diacetamido-2,4,6-trideoxy-beta-L-altropyranose.
CC {ECO:0000269|PubMed:16728396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose = 2,4-
CC diacetamido-2,4,6-trideoxy-beta-L-altrose + H(+) + UDP;
CC Xref=Rhea:RHEA:31803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:63283, ChEBI:CHEBI:63417; EC=3.6.1.57;
CC Evidence={ECO:0000269|PubMed:16728396};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=174 uM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
CC {ECO:0000269|PubMed:16728396};
CC KM=250 uM for UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose
CC {ECO:0000269|PubMed:19483088};
CC Note=kcat is 27 sec(-1) (PubMed:16728396). kcat is 25 sec(-1)
CC (PubMed:19483088). {ECO:0000269|PubMed:16728396,
CC ECO:0000269|PubMed:19483088};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19483088}.
CC -!- SIMILARITY: Belongs to the PseG family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35426.1; -; Genomic_DNA.
DR PIR; E81274; E81274.
DR RefSeq; WP_002830499.1; NC_002163.1.
DR RefSeq; YP_002344702.1; NC_002163.1.
DR PDB; 3HBM; X-ray; 1.80 A; A=1-274.
DR PDB; 3HBN; X-ray; 1.85 A; A=1-274.
DR PDBsum; 3HBM; -.
DR PDBsum; 3HBN; -.
DR AlphaFoldDB; Q0P8U5; -.
DR SMR; Q0P8U5; -.
DR IntAct; Q0P8U5; 6.
DR STRING; 192222.Cj1312; -.
DR PaxDb; Q0P8U5; -.
DR PRIDE; Q0P8U5; -.
DR EnsemblBacteria; CAL35426; CAL35426; Cj1312.
DR GeneID; 905604; -.
DR KEGG; cje:Cj1312; -.
DR PATRIC; fig|192222.6.peg.1294; -.
DR eggNOG; COG3980; Bacteria.
DR HOGENOM; CLU_023406_0_0_7; -.
DR OMA; YEVEYRY; -.
DR BRENDA; 3.6.1.57; 1087.
DR EvolutionaryTrace; Q0P8U5; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR020023; PseG.
DR TIGRFAMs; TIGR03590; PseG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..274
FT /note="UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-
FT altropyranose hydrolase"
FT /id="PRO_0000418931"
FT ACT_SITE 17
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:19483088"
FT BINDING 15..16
FT /ligand="substrate"
FT BINDING 143
FT /ligand="substrate"
FT BINDING 234..235
FT /ligand="substrate"
FT BINDING 239
FT /ligand="substrate"
FT MUTAGEN 17
FT /note="H->F,L: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:19483088"
FT MUTAGEN 17
FT /note="H->N: Strongly impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:19483088"
FT MUTAGEN 78
FT /note="Y->F: Impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:19483088"
FT MUTAGEN 255
FT /note="N->A: Impaired catalytic activity."
FT /evidence="ECO:0000269|PubMed:19483088"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3HBM"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3HBM"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3HBN"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3HBM"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:3HBM"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3HBM"
SQ SEQUENCE 274 AA; 31319 MW; A65BF88D58502257 CRC64;
MKVLFRSDSS SQIGFGHIKR DLVLAKQYSD VSFACLPLEG SLIDEIPYPV YELSSESIYE
LINLIKEEKF ELLIIDHYGI SVDDEKLIKL ETGVKILSFD DEIKPHHCDI LLNVNAYAKA
SDYEGLVPFK CEVRCGFSYA LIREEFYQEA KENREKKYDF FICMGGTDIK NLSLQIASEL
PKTKIISIAT SSSNPNLKKL QKFAKLHNNI RLFIDHENIA KLMNESNKLI ISASSLVNEA
LLLKANFKAI CYVKNQESTA TWLAKKGYEV EYKY
