ID   PSEI_HELPY              Reviewed;         340 AA.
AC   O24980;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Pseudaminic acid synthase;
DE            EC=2.5.1.97;
DE   AltName: Full=Pseudaminic acid biosynthesis protein I;
GN   Name=pseI; OrderedLocusNames=HP_0178;
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   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   [3]
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).
CC   -!- FUNCTION: Catalyzes the fifth step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Catalyzes the condensation of phosphoenolpyruvate with 2,4-diacetamido-
CC       2,4,6-trideoxy-beta-l-altropyranose, forming pseudaminic acid (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose + H2O +
CC         phosphoenolpyruvate = phosphate + pseudaminate; Xref=Rhea:RHEA:31631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:63282, ChEBI:CHEBI:63283; EC=2.5.1.97;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the pseudaminic acid synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000511; AAD07248.1; -; Genomic_DNA.
DR   PIR; B64542; B64542.
DR   RefSeq; NP_206977.1; NC_000915.1.
DR   RefSeq; WP_000941291.1; NC_018939.1.
DR   AlphaFoldDB; O24980; -.
DR   SMR; O24980; -.
DR   DIP; DIP-3369N; -.
DR   IntAct; O24980; 6.
DR   MINT; O24980; -.
DR   STRING; 85962.C694_00885; -.
DR   PaxDb; O24980; -.
DR   EnsemblBacteria; AAD07248; AAD07248; HP_0178.
DR   KEGG; hpy:HP_0178; -.
DR   PATRIC; fig|85962.47.peg.193; -.
DR   eggNOG; COG2089; Bacteria.
DR   OMA; YRHRVEF; -.
DR   PhylomeDB; O24980; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR036732; AFP_Neu5c_C_sf.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013132; Neu5Ac_N.
DR   InterPro; IPR020030; Pseudaminic_synth_PseI.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF03102; NeuB; 1.
DR   Pfam; PF08666; SAF; 1.
DR   SMART; SM00858; SAF; 1.
DR   SUPFAM; SSF51269; SSF51269; 1.
DR   TIGRFAMs; TIGR03586; PseI; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..340
FT                   /note="Pseudaminic acid synthase"
FT                   /id="PRO_0000418933"
FT   DOMAIN          281..337
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ   SEQUENCE   340 AA;  38007 MW;  E2880092AFAC77F7 CRC64;
     MLQPPKIVAE LSANHNQDLN LAKESLHAIK ESGADFVKLQ TYTPSCMTLN SKEDPFIIQG
     TLWDKENLYE LYQKASTPLE WHAELFELAR KLDLGIFSSP FSSQALELLE SLNCPMYKIA
     SFEIVDLDLI EKAARTQKPI ILSSGIATHT ELQDAISLCR RVNNFDITLL KCVSAYPSKI
     EDANLLSMVK LGEIFGVKFG LSDHTIGSLC PILATTLGAS MIEKHFILNK SLQTPDSAFS
     MDFNGFKSMV EAIKQSVLAL GEEEPRINPK TLEKRRFFAR SLFVIKDIQK GEALTENNIK
     ALRPNLGLHP KFYKEILGQK ASKFLKANTP LSADDIERSL