ID   F2R5T3_STRVP            Unreviewed;       669 AA.
AC   F2R5T3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   OrderedLocusNames=SVEN_0307 {ECO:0000313|EMBL:CCA53594.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53594.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA53594.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; FR845719; CCA53594.1; -; Genomic_DNA.
DR   RefSeq; WP_015031513.1; NZ_JABVZO010000295.1.
DR   AlphaFoldDB; F2R5T3; -.
DR   STRING; 953739.SVEN_0307; -.
DR   GeneID; 69862524; -.
DR   KEGG; sve:SVEN_0307; -.
DR   PATRIC; fig|953739.5.peg.5874; -.
DR   eggNOG; COG4409; Bacteria.
DR   HOGENOM; CLU_430157_0_0_11; -.
DR   OrthoDB; 7294637at2; -.
DR   Proteomes; UP000006854; Chromosome.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00110; LamG; 1.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006558; LamG-like.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:CCA53594.1};
KW   Hydrolase {ECO:0000313|EMBL:CCA53594.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           45..669
FT                   /note="exo-alpha-sialidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003288968"
FT   DOMAIN          489..642
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          489..637
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
SQ   SEQUENCE   669 AA;  70644 MW;  D2BE42533132A658 CRC64;
     MTSLSERRPP DARRFARSAW LCALALTLLA AVAFAVSPPS PATAATAGTT TPPLATQVSN
     TPFKARENYY CTRIPALVTS TKGVLLAFAE GRNRLTTTGC HDVGDNDLVL KRSLDGGATW
     QALQVVVGAG DELAHGNPAP VVDAVSGRIT LLYSSSEWNH DGAKPSRAGY ARTVHAIHST
     DDGATWSASV PQPQLKAAGW GWVSTGPGHG IQLGRGPHHG RLIVPGDHTA GGDTTAGGQL
     YISDNGGLTW AIGARSESAK SGAYPGELTV AQTVDGGVYV NARNSEPTRC LTNEHRLETV
     SPDGGDSFAA PFTPVANLDT SPVFGSLLRL HAQDQDAKPN RLLYSGASRL GPSPLEDRRE
     LAIRSSYDEG KTWRTVGTLV SAARTGYSDL TLLPSGSIGI LYETAGNIPH GNVAFGAFTE
     QAMQDSETEL RRPRTGDTHV RAAGEAGNHA IVHGGARLGT RHDGVAMEFD GQDDYLRLVC
     SPSLRVDDKD FTVTAWFRHS AATGTLPIIW AYGMPGTDPL KKGRHFSVRA EPGGNLLRAT
     VGTDIGSTEV TLPSSYNDGT WHHVVFTRQG LTIGLAVDGQ PAATATMPAG NSAADRNVTP
     AAEFNIHIGA RPDFPNQPAG VAQLFHGTLD DVRLFRTALT DAEAARVKAG ALDVATDREK
     LRLGFTTIW
//