C1437_CAMJE
ID C1437_CAMJE Reviewed; 367 AA.
AC Q0P8H7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Dihydroxyacetone phosphate transaminase Cj1437c {ECO:0000305|PubMed:34505775};
DE EC=2.6.1.- {ECO:0000269|PubMed:34505775};
DE AltName: Full=Capsule polysaccharide biosynthesis protein Cj1437c {ECO:0000305|PubMed:34505775};
DE AltName: Full=PLP-dependent transaminase Cj1437 {ECO:0000303|PubMed:34505775};
GN OrderedLocusNames=Cj1437c {ECO:0000312|EMBL:CAL35546.1};
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:CAL35546.1, 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, PATHWAY, AND BIOTECHNOLOGY.
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 transaminase involved in
CC the biosynthesis of amidated D-glucuronic acid structures found on the
CC capsular polysaccharide (CPS) of C.jejuni. Catalyzes the transamination
CC of dihydroxyacetone phosphate (DHAP) to (S)-serinol phosphate in the
CC presence of L-glutamate. Less active with L-aspartate. No activity with
CC dihydroxyacetone or L-alanine. {ECO:0000269|PubMed:34505775}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + L-glutamate = (S)-serinol
CC phosphate + 2-oxoglutarate; Xref=Rhea:RHEA:69552, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57642, ChEBI:CHEBI:184377;
CC Evidence={ECO:0000269|PubMed:34505775};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|RuleBase:RU003693,
CC ECO:0000269|PubMed:34505775};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for dihydroxyacetone phosphate (DHAP) (at pH 8.0 and 25
CC degrees Celsius) {ECO:0000269|PubMed:34505775};
CC Note=kcat is 0.50 sec(-1) with DHAP as substrate.
CC {ECO:0000269|PubMed:34505775};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:34505775}.
CC -!- BIOTECHNOLOGY: The reaction product of this enzyme, serinol phosphate,
CC is an important precursor for serinol (2-amino-1,3-propanediol)
CC production. Serinol, in turn, is an intermediate in the formation of
CC certain drugs, such as the anti-cancer N-palmitoyl-2-amino-1,3-
CC propanediol, and the orally administered fingolimod (sold under the
CC brand name Gilenya) to treat multiple sclerosis.
CC {ECO:0000305|PubMed:34505775}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|RuleBase:RU003693}.
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DR EMBL; AL111168; CAL35546.1; -; Genomic_DNA.
DR PIR; E81289; E81289.
DR RefSeq; WP_002858082.1; NC_002163.1.
DR RefSeq; YP_002344820.1; NC_002163.1.
DR AlphaFoldDB; Q0P8H7; -.
DR STRING; 192222.Cj1437c; -.
DR PaxDb; Q0P8H7; -.
DR PRIDE; Q0P8H7; -.
DR DNASU; 905726; -.
DR EnsemblBacteria; CAL35546; CAL35546; Cj1437c.
DR GeneID; 905726; -.
DR KEGG; cje:Cj1437c; -.
DR PATRIC; fig|192222.6.peg.1418; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_0_7; -.
DR OMA; FDGYPIL; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
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; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Capsule biogenesis/degradation; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Dihydroxyacetone phosphate transaminase Cj1437c"
FT /id="PRO_0000455117"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9X0D0"
SQ SEQUENCE 367 AA; 41929 MW; 38D67EC61D55FA67 CRC64;
MQANKNIQKL TPYLSIPHKI WNSSQSNILK LDWNEATIPP SPYVIESIKK FLVNGNLNWY
PNTKNLYLLD KIAEYTKQIN SSFVELFEGS DSAHECIIDV FLDKCDKIGI VSPTYDNFRS
RANGVGIETI SFTLDDNFNL DFDSLEYFIH EKRIKLLYLC NPNNPTGKSY NIQKIKSLII
NNPNVMFIID EAYYEFTSQS VCDLVEQCNN LIITRTFSKA FALASFRIGY IISHPENIES
INKLRNPKSV PMLSQIAANA ALEDLQYMRD YVDEVSCARM EFVKFLNTLT TGGGGIFNDS
VANFVLIQNE NISLFVGFLE KEGIFIRNYS HLISKNCRIS IGTRNQMSYV AEKIQEFAKK
QGGFHLV
