ID Q6A9X5_CUTAK Unreviewed; 771 AA. AC Q6A9X5; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733}; DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733}; GN OrderedLocusNames=PPA0685 {ECO:0000313|EMBL:AAT82441.1}; OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium OS acnes). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Propionibacteriaceae; Cutibacterium. OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT82441.1, ECO:0000313|Proteomes:UP000000603}; RN [1] {ECO:0000313|EMBL:AAT82441.1, ECO:0000313|Proteomes:UP000000603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603}; RX PubMed=15286373; DOI=10.1126/science.1100330; RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., RA Strittmatter A., Hujer S., Durre P., Gottschalk G.; RT "The complete genome sequence of Propionibacterium acnes, a commensal of RT human skin."; RL Science 305:671-673(2004). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. CC {ECO:0000256|ARBA:ARBA00009348}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017283; AAT82441.1; -; Genomic_DNA. DR RefSeq; WP_002515306.1; NZ_CP025935.1. DR AlphaFoldDB; Q6A9X5; -. DR SMR; Q6A9X5; -. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR EnsemblBacteria; AAT82441; AAT82441; PPA0685. DR KEGG; pac:PPA0685; -. DR PATRIC; fig|267747.3.peg.718; -. DR eggNOG; COG4409; Bacteria. DR HOGENOM; CLU_368301_0_0_11; -. DR Proteomes; UP000000603; 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; 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; 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; PF13088; BNR_2; 1. DR Pfam; PF13385; Laminin_G_3; 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:AAT82441.1}; KW Hydrolase {ECO:0000313|EMBL:AAT82441.1}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 481..728 FT /note="Sialidase" FT /evidence="ECO:0000259|Pfam:PF13088" SQ SEQUENCE 771 AA; 83652 MW; DBD0A907B0DE43B8 CRC64; MTITDTYTEE LAIDLTGSAL LPARKGMDVQ RIDGEDGSLL VEFSATSSGC LFELVGKNGR LSVDVDEDRL LGRIDLNGES RSLDAEDALG MADGTIHSVG LTADETGTHL FADGYETFSA TLRVWCQDLG ATNIVINPSG VLDVRRFKMW NSALSLQAMA AKAPTATPFV EFAGSELSAR DARRIGELAH GALRARTRLR GKGQGGTVLA AQGSAGELSF EIVNGDLLLH VEVDDEPIAH VRAPGKWDDG NWHDLVAISG RGAIDLYVDG FLVAHEPGEA FFADLGKVER VTVGKDLEGA RLFGEAQTAS IFSSALTDAQ VKRLANVAPL RTQALFDTGY LGSKSYRIPS LIRLDSGSFI AGADQRVSIA NDSPNDINFV IRRSEDGRRW DEAQIVLEYP GEGALGASVI DSVLFQDHNS GRVFCLIDQF PGGVGQPNAE PGSGFDEQGR QLLFDRDATA YVIDAEGIVT TESGEPTDYT VDETGNVFAA GAPAGNIHLA TGVDPHESLL TLRTCNLILI HSDDDGRTWS RPINLNPALK QPWMRFLGTS PGNGIQLEHG THRGRLLAPV YYNHEEGKTF SCAAVYSDDG GQTWNLGKSP NDERELFGKI VSSRNLNDDR GSTHESALVE TPDGVVHSFM RNQHPSGRVA HAASVDGGET WGEVTFVEQL TEIFSQPNAI SVRDELGTES VVFANASMML PFRGCGVLRQ SFDGGKTWPH NRVLNPRHHV YQCMTQQDEQ TLLVLWEREW QGLFLTEVPL SWLTTSRSTL E //