ID A0A7X3IEJ4_9BACL Unreviewed; 729 AA.
AC A0A7X3IEJ4;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN ORFNames=GRF59_02380 {ECO:0000313|EMBL:MWV42468.1};
OS Paenibacillus dendrobii.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2691084 {ECO:0000313|EMBL:MWV42468.1, ECO:0000313|Proteomes:UP000460318};
RN [1] {ECO:0000313|EMBL:MWV42468.1, ECO:0000313|Proteomes:UP000460318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJL G12 {ECO:0000313|EMBL:MWV42468.1,
RC ECO:0000313|Proteomes:UP000460318};
RA Zhao R.;
RT "Paenibacillus sp. nov., an endophytic bacterium isolated from the stem of
RT Dendrobium.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000427};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MWV42468.1}.
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DR EMBL; WUBI01000001; MWV42468.1; -; Genomic_DNA.
DR RefSeq; WP_160496066.1; NZ_WUBI01000001.1.
DR AlphaFoldDB; A0A7X3IEJ4; -.
DR Proteomes; UP000460318; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006689; P:ganglioside catabolic process; IEA:TreeGrafter.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR004124; Glyco_hydro_33_N.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628:SF30; EXO-ALPHA-SIALIDASE; 1.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF02973; Sialidase; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000460318};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..729
FT /note="exo-alpha-sialidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039719193"
FT DOMAIN 65..197
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT DOMAIN 244..376
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
SQ SEQUENCE 729 AA; 78556 MW; AE2F2A96AF5915D3 CRC64;
MKCGHMLRIV LGASLLASSI VGLAQTAKAS LSDGLVLDYT LNRAFNGMSE FVDKTADLGT
VSGLSQGSVA VKFKTTSTAQ AKTFLSASDT SDPSSNLSFT MNNGTVYFEN RENGVYATQI
SASGAYNDGS WHTAVLTVNS SGTKMYVDGS IKGTSDSTAF MLNVTNLNGM WVGKNVDNGG
SQWFYGGEMD YVKVYNRALT DTEAQQLAGT LPDLVATYTI HQSFNGTSDF LDKTGDLSVV
SGLSQGAIAV KFKTTSTAQA KTFLSASDTS DPSSNISFTM NNGTVYFENR ENNAYATRIS
AAGTYNDGNW HTAILNVGST GSKIYIDGYE KVTSPSIAFF TNVTNLSGMW VGKNVDNGGS
QWFYNGELDF INLYSNPLSD NQIKQISSTF QDTILFDIND GKGYAQYRIP SIAVMTDGTV
LTVVEGRSGG DQTPTDLVLR RSTDGGKTFS DNVILAPGKS QGFAEMNPML LAENTGSTVH
LLWSRWKWGN CQYFIRTSHD NGVTWDAARD ITSVLNAYKD PANPNYFANL SGAGMGPGHG
IQLKDGTLMV PIYFTTPNWT NSTVATIYSN DGGLTWQAGT KVPNPSGFTK IHENMMVELS
DGSLMANMRN PGSNYRAIST SSGVTGAWST PHSDQVLIDP VNEASIQRYD DSTILFTNAA
NSSSRTHMTI RMSNDDGATW YKSKEIYAGS NGYSDIGVSS NKTIYVFYEK PASQKIALAI
FNKAWVEAP
//
