ID   PSEI_CAMJE              Reviewed;         343 AA.
AC   Q0P8U0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Pseudaminic acid synthase;
DE            EC=2.5.1.97;
DE   AltName: Full=Pseudaminic acid biosynthesis protein I;
GN   Name=pseI; Synonyms=neuB3; OrderedLocusNames=Cj1317;
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, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=16120604; DOI=10.1074/jbc.m507483200;
RA   Chou W.K., Dick S., Wakarchuk W.W., Tanner M.E.;
RT   "Identification and characterization of NeuB3 from Campylobacter jejuni as
RT   a pseudaminic acid synthase.";
RL   J. Biol. Chem. 280:35922-35928(2005).
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.
CC       {ECO:0000269|PubMed:16120604}.
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         Evidence={ECO:0000269|PubMed:16120604};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:16120604};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.5 uM for phosphoenolpyruvate {ECO:0000269|PubMed:16120604};
CC         KM=9.5 uM for 6-deoxy-AltdiNAc {ECO:0000269|PubMed:16120604};
CC         Note=kcat is 0.65 sec(-1).;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:16120604};
CC   -!- SIMILARITY: Belongs to the pseudaminic acid synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AL111168; CAL35431.1; -; Genomic_DNA.
DR   PIR; B81275; B81275.
DR   RefSeq; WP_002870258.1; NC_002163.1.
DR   RefSeq; YP_002344707.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8U0; -.
DR   SMR; Q0P8U0; -.
DR   IntAct; Q0P8U0; 20.
DR   STRING; 192222.Cj1317; -.
DR   PaxDb; Q0P8U0; -.
DR   PRIDE; Q0P8U0; -.
DR   EnsemblBacteria; CAL35431; CAL35431; Cj1317.
DR   GeneID; 905609; -.
DR   KEGG; cje:Cj1317; -.
DR   PATRIC; fig|192222.6.peg.1299; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_1_7; -.
DR   OMA; CWDEEAV; -.
DR   BioCyc; MetaCyc:MON-14522; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..343
FT                   /note="Pseudaminic acid synthase"
FT                   /id="PRO_0000418934"
FT   DOMAIN          287..343
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ   SEQUENCE   343 AA;  38647 MW;  45B4E9DB243BDB8B CRC64;
     MQIGNFNTDK KVFIIAELSA NHAGSLEMAL KSIKAAKKAG ADAIKIQTYT PDSLTLNSDK
     EDFIIKGGLW DKRKLYELYE SAKTPYEWHS QIFETAQNEG ILCFSSPFAK EDVEFLKRFD
     PIAYKIASFE ANDENFVRLI AKEKKPTIVS TGIATEEELF KICEIFKEEK NPDLVFLKCT
     STYPTAIEDM NLKGIVSLKE KFNVEVGLSD HSFGFLAPVM AVALGARVIE KHFMLDKSIE
     SEDSKFSLDF DEFKAMVDAV RQAESALGDG KLDLDEKVLK NRVFARSLYA SKDIKKGEMF
     SEENVKSVRP SFGLHPKFYQ ELLGKKASKD IKFGDALKQG DFQ