NANH_SALTY
ID NANH_SALTY Reviewed; 382 AA.
AC P29768;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sialidase;
DE EC=3.2.1.18;
DE AltName: Full=N-acylneuraminate glycohydrolase;
DE AltName: Full=Neuraminidase;
DE Short=NANase;
DE AltName: Full=STNA;
GN Name=nanH; OrderedLocusNames=STM0928;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-40.
RC STRAIN=LT2;
RX PubMed=1602967; DOI=10.1111/j.1365-2958.1992.tb01538.x;
RA Hoyer L.L., Hamilton A.C., Steenbergen S.M., Vimr E.R.;
RT "Cloning, sequencing and distribution of the Salmonella typhimurium LT2
RT sialidase gene, nanH, provides evidence for interspecies gene transfer.";
RL Mol. Microbiol. 6:873-884(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC STRAIN=LT2;
RX PubMed=1518058; DOI=10.1016/0022-2836(92)91069-2;
RA Taylor G.L., Vimr E.R., Garman E.F., Laver W.G.;
RT "Purification, crystallization and preliminary crystallographic study of
RT neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2.";
RL J. Mol. Biol. 226:1287-1290(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=LT2;
RX PubMed=8234325; DOI=10.1073/pnas.90.21.9852;
RA Crennell S.J., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.;
RT "Crystal structure of a bacterial sialidase (from Salmonella typhimurium
RT LT2) shows the same fold as an influenza virus neuraminidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9852-9856(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RC STRAIN=LT2;
RX PubMed=8656428; DOI=10.1006/jmbi.1996.0318;
RA Crennell S.J., Garman E.F., Philippon C., Vasella A., Laver W.G.,
RA Vimr E.R., Taylor G.L.;
RT "The structures of Salmonella typhimurium LT2 neuraminidase and its
RT complexes with three inhibitors at high resolution.";
RL J. Mol. Biol. 259:264-280(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RA Garman E.F., Wouters J., Schneider T.R., Vimr E.R., Laver W.G.,
RA Sheldrick G.M.;
RL Submitted (JUL-1998) to the PDB data bank.
CC -!- FUNCTION: Cleaves the terminal sialic acid (N-acetyl neuraminic acid)
CC from carbohydrate chains in glycoproteins providing free sialic acid
CC which can be used as carbon and energy sources. Sialidases have been
CC suggested to be pathogenic factors in microbial infections.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL19864.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M55342; AAA27168.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19864.1; ALT_INIT; Genomic_DNA.
DR PDB; 1DIL; X-ray; 1.90 A; A=2-382.
DR PDB; 1DIM; X-ray; 1.60 A; A=2-382.
DR PDB; 2SIL; X-ray; 1.60 A; A=2-382.
DR PDB; 2SIM; X-ray; 1.60 A; A=2-382.
DR PDB; 3SIL; X-ray; 1.05 A; A=4-382.
DR PDB; 6TRG; X-ray; 1.00 A; XXX=4-382.
DR PDB; 6TVI; X-ray; 1.00 A; AAA=4-382.
DR PDB; 7AEY; X-ray; 0.92 A; AAA=4-382.
DR PDB; 7AF2; X-ray; 0.79 A; AAA=4-382.
DR PDBsum; 1DIL; -.
DR PDBsum; 1DIM; -.
DR PDBsum; 2SIL; -.
DR PDBsum; 2SIM; -.
DR PDBsum; 3SIL; -.
DR PDBsum; 6TRG; -.
DR PDBsum; 6TVI; -.
DR PDBsum; 7AEY; -.
DR PDBsum; 7AF2; -.
DR AlphaFoldDB; P29768; -.
DR SMR; P29768; -.
DR STRING; 99287.STM0928; -.
DR DrugBank; DB04561; 4-acetamido-2,4-didexoy-D-glycero-beta-D-galacto-octopyranosylphosphonic acid.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR PaxDb; P29768; -.
DR EnsemblBacteria; AAL19864; AAL19864; STM0928.
DR PATRIC; fig|99287.12.peg.978; -.
DR HOGENOM; CLU_667119_0_0_6; -.
DR BRENDA; 3.2.1.18; 5542.
DR EvolutionaryTrace; P29768; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IBA:GO_Central.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR008377; Sialidase_trypan.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13859; BNR_3; 1.
DR PRINTS; PR01803; TCSIALIDASE.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1602967"
FT CHAIN 2..382
FT /note="Sialidase"
FT /id="PRO_0000208909"
FT REPEAT 71..82
FT /note="BNR 1"
FT REPEAT 145..156
FT /note="BNR 2"
FT REPEAT 210..220
FT /note="BNR 3"
FT REPEAT 254..265
FT /note="BNR 4"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT BINDING 37
FT /ligand="substrate"
FT BINDING 246
FT /ligand="substrate"
FT BINDING 309
FT /ligand="substrate"
FT DISULFID 42..103
FT CONFLICT 329
FT /note="D -> A (in Ref. 1; AAA27168)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3SIL"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3SIL"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 111..123
FT /evidence="ECO:0007829|PDB:3SIL"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3SIL"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 204..219
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3SIL"
FT TURN 267..271
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3SIL"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:3SIL"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:3SIL"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3SIL"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:3SIL"
SQ SEQUENCE 382 AA; 42073 MW; C15515CF9C15597E CRC64;
MTVEKSVVFK AEGEHFTDQK GNTIVGSGSG GTTKYFRIPA MCTTSKGTIV VFADARHNTA
SDQSFIDTAA ARSTDGGKTW NKKIAIYNDR VNSKLSRVMD PTCIVANIQG RETILVMVGK
WNNNDKTWGA YRDKAPDTDW DLVLYKSTDD GVTFSKVETN IHDIVTKNGT ISAMLGGVGS
GLQLNDGKLV FPVQMVRTKN ITTVLNTSFI YSTDGITWSL PSGYCEGFGS ENNIIEFNAS
LVNNIRNSGL RRSFETKDFG KTWTEFPPMD KKVDNRNHGV QGSTITIPSG NKLVAAHSSA
QNKNNDYTRS DISLYAHNLY SGEVKLIDDF YPKVGNASGA GYSCLSYRKN VDKETLYVVY
EANGSIEFQD LSRHLPVIKS YN
