LST_HAEIN
ID LST_HAEIN Reviewed; 304 AA.
AC Q48211; O05084;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase {ECO:0000305|PubMed:11842084};
DE EC=2.4.99.6 {ECO:0000250|UniProtKB:P72097, ECO:0000305|PubMed:11842084};
DE AltName: Full=CMP-N-acetylneuraminate:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000305|PubMed:11842084};
DE Short=CMP-Neu5Ac:beta-galactoside alpha-2,3-sialyltransferase {ECO:0000305|PubMed:11842084};
DE AltName: Full=Lipooligosaccharide sialyltransferase {ECO:0000303|PubMed:11842084};
DE Short=LOS sialyltransferase {ECO:0000303|PubMed:11842084};
GN Name=lsgB {ECO:0000303|PubMed:11842084}; OrderedLocusNames=HI_1699;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2;
RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.;
RT "Characterization and sequence of the lsg locus from Haemophilus
RT influenzae.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=A2;
RX PubMed=11842084; DOI=10.1074/jbc.m110986200;
RA Jones P.A., Samuels N.M., Phillips N.J., Munson R.S. Jr., Bozue J.A.,
RA Arseneau J.A., Nichols W.A., Zaleski A., Gibson B.W., Apicella M.A.;
RT "Haemophilus influenzae type b strain A2 has multiple sialyltransferases
RT involved in lipooligosaccharide sialylation.";
RL J. Biol. Chem. 277:14598-14611(2002).
CC -!- FUNCTION: Catalyzes the transfer of sialic acid from the substrate CMP-
CC N-acetylneuraminate to the terminal galactose residue of the N-
CC acetyllactosamine moiety of surface lipooligosaccharide (LOS). Thus,
CC functions in the sialylation of LOS, which plays a role in the evasion
CC of the host immune response. {ECO:0000269|PubMed:11842084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC Evidence={ECO:0000250|UniProtKB:P72097, ECO:0000305|PubMed:11842084};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide
CC biosynthesis. {ECO:0000269|PubMed:11842084}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene results in persistence of
CC sialylated glycoforms of lipooligosaccharide but a reduction in sialyl-
CC N-acetyllactosamine-containing glycoforms.
CC {ECO:0000269|PubMed:11842084}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 family.
CC {ECO:0000305}.
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DR EMBL; M94855; AAA24979.1; -; Genomic_DNA.
DR EMBL; L42023; AAC23345.1; -; Genomic_DNA.
DR PIR; G64175; G64175.
DR RefSeq; NP_439841.1; NC_000907.1.
DR AlphaFoldDB; Q48211; -.
DR SMR; Q48211; -.
DR STRING; 71421.HI_1699; -.
DR CAZy; GT52; Glycosyltransferase Family 52.
DR EnsemblBacteria; AAC23345; AAC23345; HI_1699.
DR KEGG; hin:HI_1699; -.
DR PATRIC; fig|71421.8.peg.1778; -.
DR eggNOG; ENOG502ZAT3; Bacteria.
DR HOGENOM; CLU_076077_0_0_6; -.
DR BioCyc; HINF71421:G1GJ1-1715-MON; -.
DR UniPathway; UPA00501; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR012477; Glyco_transf_52.
DR Pfam; PF07922; Glyco_transf_52; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..304
FT /note="N-acetyllactosaminide alpha-2,3-sialyltransferase"
FT /id="PRO_0000080571"
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 CONFLICT 4
FT /note="M -> I (in Ref. 1; AAA24979)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="F -> S (in Ref. 1; AAA24979)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="G -> D (in Ref. 1; AAA24979)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="Y -> C (in Ref. 1; AAA24979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 35706 MW; B6D03890AC1CDD28 CRC64;
MNLMLCCTPL QVLIARKIIE LHPNEQFFGV MFGGVWDKKR TLYASKLAEV CSDSMNIDTG
KDLKGFDFLK LMRQLKNKIT HKGFDKVFLA NLNSLWLQTY LSHVSFKELY TFDDGSDNIF
PHPNLLREPG TFKYKLIKAF IGDKYSVNKL FKKIKKHYTV YPNYKNIVSN IEPISLWDNQ
IDCEIDGEVS FFIGQPLLNT KEENISLIKK LKDQIPFDYY FPHPAEDYRV DGVNYVESEL
IFEDYVFKHL SNKKIIIYTF FSSVAFNLLS HPNVEIRFIR TSIPRWQFCY DSFPDLGLTI
YKEI
