PSEB_HELPY
ID PSEB_HELPY Reviewed; 333 AA.
AC O25511;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=UDP-N-acetylglucosamine 4,6-dehydratase (inverting);
DE EC=4.2.1.115;
DE AltName: Full=Pseudaminic acid biosynthesis protein B;
DE AltName: Full=UDP-GlcNAc-inverting 4,6-dehydratase;
GN Name=pseB; Synonyms=flaA1; OrderedLocusNames=HP_0840;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10954725; DOI=10.1074/jbc.m006369200;
RA Creuzenet C., Schur M.J., Li J., Wakarchuk W.W., Lam J.S.;
RT "FlaA1, a new bifunctional UDP-GlcNAc C6 Dehydratase/ C4 reductase from
RT Helicobacter pylori.";
RL J. Biol. Chem. 275:34873-34880(2000).
RN [3]
RP IDENTIFICATION.
RX PubMed=12791140; DOI=10.1046/j.1365-2958.2003.03527.x;
RA Schirm M., Soo E.C., Aubry A.J., Austin J., Thibault P., Logan S.M.;
RT "Structural, genetic and functional characterization of the flagellin
RT glycosylation process in Helicobacter pylori.";
RL Mol. Microbiol. 48:1579-1592(2003).
RN [4]
RP PATHWAY.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16751642; DOI=10.1093/glycob/cwl010;
RA Schoenhofen I.C., McNally D.J., Brisson J.R., Logan S.M.;
RT "Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori:
RT synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction.";
RL Glycobiology 16:8C-14C(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700392 / 26695;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP AND
RP UDP-D-GALACTOPYRANOSE, COFACTOR, SUBUNIT, AND MUTAGENESIS OF LYS-133.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16651261; DOI=10.1074/jbc.m602393200;
RA Ishiyama N., Creuzenet C., Miller W.L., Demendi M., Anderson E.M.,
RA Harauz G., Lam J.S., Berghuis A.M.;
RT "Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism
RT for inverting 4,6-dehydratase activity.";
RL J. Biol. Chem. 281:24489-24495(2006).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of pseudaminic
CC acid, a sialic-acid-like sugar that is used to modify flagellin. Has
CC both C6 dehydratase and C5 epimerase activities that result in the
CC production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-
CC hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose.
CC {ECO:0000269|PubMed:16286454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-
CC dideoxy-beta-L-arabino-hex-4-ulose; Xref=Rhea:RHEA:26111,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57705, ChEBI:CHEBI:60101;
CC EC=4.2.1.115; Evidence={ECO:0000269|PubMed:16286454};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:16651261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=159 uM for UDP-GlcNAc {ECO:0000269|PubMed:10954725};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16651261}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07887.1; -; Genomic_DNA.
DR PIR; H64624; H64624.
DR RefSeq; NP_207633.1; NC_000915.1.
DR RefSeq; WP_001132631.1; NC_018939.1.
DR PDB; 2GN4; X-ray; 1.90 A; A/B=1-333.
DR PDB; 2GN6; X-ray; 2.70 A; A/B=1-333.
DR PDB; 2GN8; X-ray; 2.10 A; A/B=1-333.
DR PDB; 2GN9; X-ray; 2.80 A; A/B=1-333.
DR PDB; 2GNA; X-ray; 2.60 A; A/B=1-333.
DR PDBsum; 2GN4; -.
DR PDBsum; 2GN6; -.
DR PDBsum; 2GN8; -.
DR PDBsum; 2GN9; -.
DR PDBsum; 2GNA; -.
DR AlphaFoldDB; O25511; -.
DR SMR; O25511; -.
DR IntAct; O25511; 1.
DR STRING; 85962.C694_04305; -.
DR PaxDb; O25511; -.
DR EnsemblBacteria; AAD07887; AAD07887; HP_0840.
DR KEGG; hpy:HP_0840; -.
DR PATRIC; fig|85962.8.peg.874; -.
DR eggNOG; COG1086; Bacteria.
DR OMA; HEVMIPK; -.
DR PhylomeDB; O25511; -.
DR BioCyc; MetaCyc:HP0840-MON; -.
DR SABIO-RK; O25511; -.
DR EvolutionaryTrace; O25511; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IPR020025; PseB.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03589; PseB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; NADP; Nucleotide-binding; Reference proteome.
FT CHAIN 1..333
FT /note="UDP-N-acetylglucosamine 4,6-dehydratase (inverting)"
FT /id="PRO_0000418954"
FT ACT_SITE 133
FT /evidence="ECO:0000305"
FT BINDING 19..22
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 43..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 67..68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 91
FT /ligand="substrate"
FT BINDING 129..130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 173
FT /ligand="substrate"
FT BINDING 174..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16651261"
FT BINDING 181
FT /ligand="substrate"
FT BINDING 199
FT /ligand="substrate"
FT BINDING 258
FT /ligand="substrate"
FT BINDING 261
FT /ligand="substrate"
FT MUTAGEN 133
FT /note="K->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16651261"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2GN4"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:2GN4"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2GNA"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:2GN4"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:2GN4"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:2GN4"
SQ SEQUENCE 333 AA; 37354 MW; 8EF0A39F0FBF0516 CRC64;
MPNHQNMLDN QTILITGGTG SFGKCFVRKV LDTTNAKKII VYSRDELKQS EMAMEFNDPR
MRFFIGDVRD LERLNYALEG VDICIHAAAL KHVPIAEYNP LECIKTNIMG ASNVINACLK
NAISQVIALS TDKAANPINL YGATKLCSDK LFVSANNFKG SSQTQFSVVR YGNVVGSRGS
VVPFFKKLVQ NKASEIPITD IRMTRFWITL DEGVSFVLKS LKRMHGGEIF VPKIPSMKMT
DLAKALAPNT PTKIIGIRPG EKLHEVMIPK DESHLALEFE DFFIIQPTIS FQTPKDYTLT
KLHEKGQKVA PDFEYSSHNN NQWLEPDDLL KLL
