(data stored in SCRATCH9089 zone)

SWISSPROT: 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   11-DEC-2019, entry version 90.
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}.
DR   EMBL; AE004439; AAK02592.1; -; Genomic_DNA.
DR   RefSeq; WP_010906695.1; NC_002663.1.
DR   SMR; Q9CNC4; -.
DR   CAZy; GT52; Glycosyltransferase Family 52.
DR   EnsemblBacteria; AAK02592; AAK02592; PM0508.
DR   KEGG; pmu:PM0508; -.
DR   PATRIC; fig|272843.6.peg.514; -.
DR   eggNOG; ENOG4105P7J; Bacteria.
DR   eggNOG; ENOG4111XG2; LUCA.
DR   HOGENOM; HOG000286172; -.
DR   KO; K00785; -.
DR   OMA; CCTPLQV; -.
DR   BioCyc; PMUL272843:G1FZ8-538-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   InterPro; IPR012477; Glyco_transf_52.
DR   Pfam; PF07922; Glyco_transf_52; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9CNC4.
DR   SWISS-2DPAGE; Q9CNC4.
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   REGION          221..225
FT                   /note="CMP-N-acetylneuraminate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P72097"
FT   REGION          242..243
FT                   /note="CMP-N-acetylneuraminate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P72097"
FT   REGION          262..263
FT                   /note="CMP-N-acetylneuraminate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P72097"
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   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
//

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