ID   E3D837_GARV3            Unreviewed;       907 AA.
AC   E3D837;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   OrderedLocusNames=HMPREF0421_20186 {ECO:0000313|EMBL:ADP38272.1};
OS   Gardnerella vaginalis (strain ATCC 14019 / 317).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38272.1, ECO:0000313|Proteomes:UP000001453};
RN   [1] {ECO:0000313|EMBL:ADP38272.1, ECO:0000313|Proteomes:UP000001453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA   Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA   Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA   Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT   differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; CP002104; ADP38272.1; -; Genomic_DNA.
DR   RefSeq; WP_013399386.1; NC_014644.1.
DR   RefSeq; YP_003985295.1; NC_014644.1.
DR   AlphaFoldDB; E3D837; -.
DR   SMR; E3D837; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   KEGG; gvg:HMPREF0421_20186; -.
DR   PATRIC; fig|525284.18.peg.178; -.
DR   HOGENOM; CLU_368301_0_0_11; -.
DR   OrthoDB; 7294637at2; -.
DR   Proteomes; UP000001453; Chromosome.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR002860; BNR_rpt.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR   Pfam; PF02012; BNR; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          600..814
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
FT   REGION          888..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  99756 MW;  60F7F5FAA1041E2A CRC64;
     MERRSTKTTS LIEDIADIKG SEHTRFNHAT IKITPSSEIK KYSENESGIN RKDKNEEINQ
     NEGIIGFKFV ANSDCDLLDI KPAQKSEASA QQEHTTPIIK ISIKEDAPLL SAQNLLEDSA
     DANGAKEIAL QMEDALGACD GREHDFAITY GSFGSRFYLD GYQCFASATN LGPQRVSGKA
     AEVCAAQAES SQIYDFYYSS HLPNPEEIAN SATQAQPDIW FAGPTICARD IKRVSCNSSG
     TLHIQFRLRG PGQHGVLFAA GTVGTKTNLE SSEKISVYAG PEGIKITLID SETCIKSVIE
     AAASVDDGEW HDLIIRANRG AIDIYVDGYS ESHNIGQFWF ANIPELNAVS IGEDLRGVRL
     MGEARTGGIY FSALTEGQIQ RISRVKPLVT TALFDTGYAG SRSYRIPSLV KTRMGTLIAG
     ADQRTSVSND APNHINFVIR RSTDGGKTWK PLQTVINMPG KNLGKLGASA IDSCPILDPA
     GKSERINVLI DLNPSGIGLT NCKTDVGVDE CGRIKMEDRF GRHYAALMDG SAAVKLPCDS
     SEKECATKWL VFPDGSIKNC DSHNDLRNNS HSNQTCDSST WNIWKSQEIA SESQPLFAEK
     TCYIAQIYSD DDGKTWSATR LIDHMVKEPW MSFAGVCPGN GIVIRQSEKH YGRILVPFYC
     SGKSKSHYSS GALISDDDGK TWSRGKMINE GRLINGKIVD PATMQDDDAT SSETVFVERK
     NGDILAFFRN QNRSGCVGKA ISHDCGETWS ELIFDTSLPE IFSQPSATCF NSENADNADC
     IAFANASQMM PYRGRGVVRF SYDGGKTWAK SVCINPFHHV YQCLSSSNKR TLQLLWERET
     TGIYITAIDS NLWKQDNLQI DFKSNAKSLN NTDLDCIKNK INTSEKMKDL EEGSLTRTER
     SQHGRDI
//