ID   C1436_CAMJE             Reviewed;         390 AA.
AC   Q0P8H8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=L-serine phosphate decarboxylase Cj1436c {ECO:0000305|PubMed:34505775};
DE            EC=4.1.1.- {ECO:0000269|PubMed:34505775};
DE   AltName: Full=Capsule polysaccharide biosynthesis protein Cj1436c {ECO:0000305|PubMed:34505775};
DE   AltName: Full=PLP-dependent decarboxylase Cj1436 {ECO:0000303|PubMed:34505775};
GN   OrderedLocusNames=Cj1436c {ECO:0000312|EMBL:CAL35545.1};
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 {ECO:0000312|Proteomes:UP000000799};
RN   [1] {ECO:0000312|EMBL:CAL35545.1, ECO:0000312|Proteomes:UP000000799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000312|Proteomes:UP000000799};
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, SUBSTRATE SPECIFICITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:34505775};
RX   PubMed=34505775; DOI=10.1021/acs.biochem.1c00439;
RA   Riegert A.S., Narindoshvili T., Coricello A., Richards N.G.J.,
RA   Raushel F.M.;
RT   "Functional Characterization of Two PLP-Dependent Enzymes Involved in
RT   Capsular Polysaccharide Biosynthesis from Campylobacter jejuni.";
RL   Biochemistry 60:2836-2843(2021).
CC   -!- FUNCTION: Pyridoxal phosphate (PLP)-dependent decarboxylase involved in
CC       the biosynthesis of amidated D-glucuronic acid structures found on the
CC       capsular polysaccharide (CPS) of C.jejuni. Catalyzes the
CC       decarboxylation of L-serine phosphate to ethanolamine phosphate. Less
CC       active with L-threonine phosphate. No activity with L-serine, L-
CC       threonine, L-aspartate or L-glutamate. {ECO:0000269|PubMed:34505775}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + O-phospho-L-serine = CO2 + phosphoethanolamine;
CC         Xref=Rhea:RHEA:69548, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57524, ChEBI:CHEBI:58190;
CC         Evidence={ECO:0000269|PubMed:34505775};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|RuleBase:RU000481,
CC         ECO:0000269|PubMed:34505775};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 mM for L-serine phosphate (at pH 8.0)
CC         {ECO:0000269|PubMed:34505775};
CC         Note=kcat is 0.21 sec(-1) with L-serine phosphate as substrate.
CC         {ECO:0000269|PubMed:34505775};
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC       {ECO:0000305|PubMed:34505775}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255|RuleBase:RU000481}.
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DR   EMBL; AL111168; CAL35545.1; -; Genomic_DNA.
DR   PIR; D81289; D81289.
DR   RefSeq; WP_002864382.1; NC_002163.1.
DR   RefSeq; YP_002344819.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8H8; -.
DR   IntAct; Q0P8H8; 15.
DR   STRING; 192222.Cj1436c; -.
DR   PaxDb; Q0P8H8; -.
DR   PRIDE; Q0P8H8; -.
DR   EnsemblBacteria; CAL35545; CAL35545; Cj1436c.
DR   GeneID; 905725; -.
DR   KEGG; cje:Cj1436c; -.
DR   PATRIC; fig|192222.6.peg.1417; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_2_7; -.
DR   OMA; KRVDMFP; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   Capsule biogenesis/degradation; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..390
FT                   /note="L-serine phosphate decarboxylase Cj1436c"
FT                   /id="PRO_0000455116"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X0D0"
SQ   SEQUENCE   390 AA;  45225 MW;  67E148B536001132 CRC64;
     MLIKLNDYEK NITQKIKDLK NASGSHSPSI FTMAEQIPEL NIKIDSCFLS NPYATALFLR
     YLKEELIDGQ KLRSVLEFYP SQNSIIAKTV ADFIGIDPKN VFIGNGAIEI IQAVMHNFVG
     KKIIVNIPTF SSYYEFAKSE TNVVYYQLSK EDNYNLNIEH YLNFVKNENP DSVVLINPNN
     PDGGYINYEK LRYILSELKY VKNIIIDESF IHFAYENKDY NGINIEYLFK EFHNTIIIKS
     MSKDFGVAGI RIGYAIMSED KIRGLLKNGY LWNSSGLSEY FLRLYVRKNF FDEYDKVRRE
     YIQETQTFFR KLSGIKQFKV YPSMANFALV ELLDGSSSTD FVAKMLIKYG IYMRTCNDKI
     GLEGEFIRIA SRTLEENDMV LKSICDVFKE