NANH_VIBCH
ID NANH_VIBCH Reviewed; 781 AA.
AC P0C6E9; P37060; Q9KR59;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Sialidase;
DE EC=3.2.1.18;
DE AltName: Full=Neuraminidase;
DE Short=NANase;
DE Flags: Precursor;
GN Name=nanH; OrderedLocusNames=VC_1784;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=7922030; DOI=10.1016/s0969-2126(00)00053-8;
RA Crenells S., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.;
RT "Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-
RT like domains in addition to the catalytic domain.";
RL Structure 2:535-544(1994).
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. Facilitates
CC cholera toxin binding to host intestinal epithelial cells by converting
CC cell surface polysialogangliosides to GM1 monogangliosides.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: May be controlled by sialic acid availability and a growth-
CC phase-dependent mechanism.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94933.1; ALT_INIT; Genomic_DNA.
DR PIR; E82158; E82158.
DR RefSeq; NP_231419.1; NC_002505.1.
DR RefSeq; WP_001211290.1; NZ_LT906614.1.
DR PDB; 1KIT; X-ray; 2.30 A; A=25-781.
DR PDB; 1W0O; X-ray; 1.90 A; A=1-781.
DR PDB; 1W0P; X-ray; 1.60 A; A=1-781.
DR PDB; 2W68; X-ray; 2.50 A; A/B/C=25-216.
DR PDB; 6EKS; X-ray; 1.87 A; A=25-781.
DR PDB; 6EKU; X-ray; 1.75 A; A=25-781.
DR PDBsum; 1KIT; -.
DR PDBsum; 1W0O; -.
DR PDBsum; 1W0P; -.
DR PDBsum; 2W68; -.
DR PDBsum; 6EKS; -.
DR PDBsum; 6EKU; -.
DR AlphaFoldDB; P0C6E9; -.
DR PCDDB; P0C6E9; -.
DR SMR; P0C6E9; -.
DR STRING; 243277.VC_1784; -.
DR BindingDB; P0C6E9; -.
DR ChEMBL; CHEMBL1075100; -.
DR CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR DNASU; 2613664; -.
DR EnsemblBacteria; AAF94933; AAF94933; VC_1784.
DR GeneID; 57740427; -.
DR KEGG; vch:VC_1784; -.
DR PATRIC; fig|243277.26.peg.1703; -.
DR eggNOG; COG4409; Bacteria.
DR HOGENOM; CLU_376807_0_0_6; -.
DR BRENDA; 3.2.1.18; 6626.
DR EvolutionaryTrace; P0C6E9; -.
DR PRO; PR:P0C6E9; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0033691; F:sialic acid binding; IEA:InterPro.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR015344; VCNA_lectin-like_dom.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF09264; Sial-lect-inser; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF50939; SSF50939; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Glycosidase; Hydrolase; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..781
FT /note="Sialidase"
FT /id="PRO_0000012033"
FT REPEAT 263..274
FT /note="BNR 1"
FT REPEAT 585..596
FT /note="BNR 2"
FT REPEAT 653..664
FT /note="BNR 3"
FT REPEAT 718..729
FT /note="BNR 4"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 619
FT /evidence="ECO:0000255"
FT ACT_SITE 740
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 635
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 712
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6EKU"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 94..106
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 202..213
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 257..271
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1KIT"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:1W0P"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:1W0P"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:6EKU"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 357..371
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 380..392
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 394..411
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 441..448
FT /evidence="ECO:0007829|PDB:1W0P"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1KIT"
FT STRAND 487..498
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 568..578
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 580..593
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:6EKU"
FT STRAND 604..610
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 616..624
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 630..638
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 649..661
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 663..669
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 684..689
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 695..702
FT /evidence="ECO:0007829|PDB:1W0P"
FT TURN 704..708
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 709..722
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 747..756
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:1W0P"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:1W0P"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:1W0P"
SQ SEQUENCE 781 AA; 85609 MW; FA85ED907FB20AF0 CRC64;
MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT NNGSGVLTNA
DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM KVLSGGMITN YYANGTQRVL
PIISLDSSGN LVVEFEGQTG RTVLATGTAA TEYHKFELVF LPGSNPSASF YFDGKLIRDN
IQPTASKQNM IVWGNGSSNT DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA
FAEKRVGGGD PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS
SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD QVKERSFQIA
GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD GSRKYVVTLS IDESGGLVAN
LNGVSAPIIL QSEHAKVHSF HDYELQYSAL NHTTTLFVDG QQITTWAGEV SQENNIQFGN
ADAQIDGRLH VQKIVLTQQG HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG
NASVNPGPGH GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL
PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR QQFLSKDGGI
TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT NPQGNPAGTN GRQNLGLWFS
FDEGVTWKGP IQLVNGASAY SDIYQLDSEN AIVIVETDNS NMRILRMPIT LLKQKLTLSQ
N
