LST_PASMU
ID LST_PASMU Reviewed; 308 AA.
AC Q9CNC4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000305|PubMed:21515586};
DE Short=CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000305|PubMed:21515586};
DE EC=2.4.99.- {ECO:0000269|PubMed:21515586};
DE AltName: Full=Glycolipid alpha-2,3-sialyltransferase {ECO:0000303|PubMed:21515586};
DE AltName: Full=PmST2 {ECO:0000303|PubMed:21515586};
GN Name=lst; OrderedLocusNames=PM0508;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 15742 / P1059;
RX PubMed=21515586; DOI=10.1093/glycob/cwr054;
RA Thon V., Lau K., Yu H., Tran B.K., Chen X.;
RT "PmST2: a novel Pasteurella multocida glycolipid alpha2-3-
RT sialyltransferase.";
RL Glycobiology 21:1206-1216(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: Catalyzes the transfer of sialic acid from the substrate CMP-
CC N-acetylneuraminate to lactosyl lipids as preferred acceptor substrates
CC in vitro, forming alpha-2,3-linked sialosides. Beta-1,4-linked
CC galactosyl lipids are better substrates than beta-1,3-linked galactosyl
CC lipids. The natural acceptor substrate may be cell surface
CC oligosaccharides in lipooligosaccharide (LOS), whose sialylation has
CC been demonstrated vital for the virulence of P.multocida.
CC {ECO:0000269|PubMed:21515586}.
CC -!- COFACTOR:
CC Note=Divalent metal cations are not required for the alpha-2,3-
CC sialyltransferase activity. {ECO:0000269|PubMed:21515586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for CMP-N-acetylneuraminate {ECO:0000269|PubMed:21515586};
CC KM=4.1 mM for Lac-beta-Pro-triazole-C14
CC {ECO:0000269|PubMed:21515586};
CC KM=28 mM for Lac-beta-Pro-2AA {ECO:0000269|PubMed:21515586};
CC Note=kcat is 12 sec(-1) for the sialylation of Lac-beta-Pro-triazole-
CC C14. kcat is 7.9 sec(-1) for the sialylation of Lac-beta-Pro-2AA.
CC {ECO:0000269|PubMed:21515586};
CC pH dependence:
CC Optimum pH is 6.0. Active in a broad pH range of 4.5-10.0. Low
CC activity is found at pH 10.0 and no significant activity is found at
CC pH 4.0. {ECO:0000269|PubMed:21515586};
CC -!- BIOTECHNOLOGY: Has been used successfully in the preparative scale
CC synthesis of sialyllactosyl sphingosine (lyso-GM3), which is an
CC important glycolipid and an intermediate for synthesizing more complex
CC glycolipids such as gangliosides. {ECO:0000269|PubMed:21515586}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family.
CC {ECO:0000305}.
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DR EMBL; AE004439; AAK02592.1; -; Genomic_DNA.
DR RefSeq; WP_010906695.1; NC_002663.1.
DR AlphaFoldDB; Q9CNC4; -.
DR SMR; Q9CNC4; -.
DR STRING; 747.DR93_1283; -.
DR CAZy; GT52; Glycosyltransferase Family 52.
DR EnsemblBacteria; AAK02592; AAK02592; PM0508.
DR KEGG; pmu:PM0508; -.
DR PATRIC; fig|272843.6.peg.514; -.
DR HOGENOM; CLU_076077_0_0_6; -.
DR OMA; CCTPLQV; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR012477; Glyco_transf_52.
DR Pfam; PF07922; Glyco_transf_52; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..308
FT /note="CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-
FT sialyltransferase"
FT /id="PRO_0000080575"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 221..225
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 242..243
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT BINDING 262..263
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:P72097"
FT VARIANT 25
FT /note="M -> T (in strain: ATCC 15742 / P1059)"
SQ SEQUENCE 308 AA; 35724 MW; E56E923367EB22C7 CRC64;
MNLIICCTPL QVLIAEKIIA KFPHMPFYGV MLSTVSNKKF DFYAKRLAQQ CQGFFSMVQH
KDRFNLLKEI LYLKRTFSGK HFDQVFVANI NDLQIQFLLS AIDFNLLNTF DDGTINIVPN
SLFYQDDPAT LQRKLINVLL GNKYSIQSLR ALSHTHYTIY KGFKNIIERV EPIELVAADN
SEKVTSAVIN VLLGQPVFAE DERNIALAER VIKQFNIHYY LPHPREKYRL AQVNYIDTEL
IFEDYILQQC QTHKYCVYTY FSSAIINIMN KSDNIEVVAL KIDTENPAYD ACYDLFDELG
VNVIDIRE
