ID NANL_MACDE Reviewed; 762 AA. AC Q27701; Q9TWN0; Q9TWN1; Q9TWN2; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 116. DE RecName: Full=Anhydrosialidase; DE EC=4.2.2.15; DE AltName: Full=Anhydroneuraminidase; DE AltName: Full=Sialidase L; DE Flags: Precursor; OS Macrobdella decora (North American leech). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata; OC Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Macrobdella. OX NCBI_TaxID=6405; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8702601; DOI=10.1074/jbc.271.32.19219; RA Chou M.-Y., Li S.-C., Li Y.-T.; RT "Cloning and expression of sialidase L, a NeuAc-alpha2-->3Gal-specific RT sialidase from the leech, Macrobdella decora."; RL J. Biol. Chem. 271:19219-19224(1996). RN [2] RP PROTEIN SEQUENCE OF 89-104; 330-338; 346-352; 387-406; 429-435; 438-469 AND RP 512-530, AND CHARACTERIZATION. RX PubMed=8034634; DOI=10.1016/s0021-9258(17)32240-8; RA Chou M.-Y., Li S.-C., Kiso M., Hasegawa A., Li Y.-T.; RT "Purification and characterization of sialidase L, a NeuAc-alpha 2-->3Gal- RT specific sialidase."; RL J. Biol. Chem. 269:18821-18826(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 81-759. RX PubMed=9562562; DOI=10.1016/s0969-2126(98)00053-7; RA Luo Y., Li S.-C., Chou M.-Y., Li Y.-T., Luo M.; RT "The crystal structure of an intramolecular trans-sialidase with a NeuAc- RT alpha2-->3Gal specificity."; RL Structure 6:521-530(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-759. RX PubMed=9878409; DOI=10.1006/jmbi.1998.2345; RA Luo Y., Li S.-C., Li Y.-T., Luo M.; RT "The 1.8 A structures of leech intramolecular trans-sialidase complexes: RT evidence of its enzymatic mechanism."; RL J. Mol. Biol. 285:323-332(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=Elimination of alpha-sialyl groups in N-acetylneuraminic acid CC glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.; CC EC=4.2.2.15; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}. 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; U46666; AAC47263.1; -; mRNA. DR PDB; 1SLI; X-ray; 2.00 A; A=81-759. DR PDB; 1SLL; X-ray; 2.00 A; A=81-759. DR PDB; 2SLI; X-ray; 1.80 A; A=81-759. DR PDB; 3SLI; X-ray; 1.80 A; A=81-759. DR PDB; 4SLI; X-ray; 1.80 A; A=81-759. DR PDBsum; 1SLI; -. DR PDBsum; 1SLL; -. DR PDBsum; 2SLI; -. DR PDBsum; 3SLI; -. DR PDBsum; 4SLI; -. DR AlphaFoldDB; Q27701; -. DR SMR; Q27701; -. DR CAZy; CBM40; Carbohydrate-Binding Module Family 40. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR EvolutionaryTrace; Q27701; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0033995; F:anhydrosialidase activity; IEA:UniProtKB-EC. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; 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; IPR013320; ConA-like_dom_sf. DR InterPro; IPR004124; Glyco_hydro_33_N. 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:SF19; SIALIDASE; 1. DR Pfam; PF13088; BNR_2; 1. DR Pfam; PF02973; Sialidase; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Lyase; KW Repeat; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..762 FT /note="Anhydrosialidase" FT /id="PRO_0000012040" FT REPEAT 328..339 FT /note="BNR 1" FT REPEAT 511..522 FT /note="BNR 2" FT REPEAT 571..582 FT /note="BNR 3" FT REPEAT 620..631 FT /note="BNR 4" FT ACT_SITE 318 FT /note="Proton acceptor" FT ACT_SITE 595 FT ACT_SITE 713 FT /note="Nucleophile" FT BINDING 293 FT /ligand="substrate" FT BINDING 611 FT /ligand="substrate" FT BINDING 673 FT /ligand="substrate" FT STRAND 83..94 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 115..125 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 147..154 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 191..198 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 232..240 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 250..260 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 264..271 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 290..299 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 305..314 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 323..332 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 372..381 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 382..385 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 386..394 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 408..412 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 415..422 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 443..446 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 447..453 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 458..461 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 467..476 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 479..490 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 507..515 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 527..529 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 541..543 FT /evidence="ECO:0007829|PDB:2SLI" FT TURN 551..554 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 556..565 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 567..575 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 581..584 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 596..600 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 606..610 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 613..616 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 618..624 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 648..656 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 659..667 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 670..674 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 676..685 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 693..705 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 714..718 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 720..722 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 724..729 FT /evidence="ECO:0007829|PDB:2SLI" FT STRAND 745..750 FT /evidence="ECO:0007829|PDB:2SLI" FT HELIX 752..755 FT /evidence="ECO:0007829|PDB:2SLI" SQ SEQUENCE 762 AA; 82982 MW; C0C547C7A8632B37 CRC64; MGRIGKKAMA IALVSAVMVT PLNVCATVEN QEQQQVTQGA EDIAVIDDAQ ETVAADEAQA DEAAAITVEG RETAEESSAS IPEGILMEKN NVDIAEGQGY SLDQEAGAKY VKAMTQGTII LSYKSTSENG IQSLFSVGNS TAGNQDRHFH IYITNSGGIG IELRNTDGVF NYTLDRPASV RALYKGERVF NTVALKADAA NKQCRLFANG ELLATLDKDA FKFISDITGV DNVTLGGTKR QGKIAYPFGG TIGDIKVYSN ALSDEELIQA TGVTTYGENI FYAGDVTESN YFRIPSLLTL STGTVISAAD ARYGGTHDSK SKINIAFAKS TDGGNTWSEP TLPLKFDDYI AKNIDWPRDS VGKNVQIQGS ASYIDPVLLE DKLTKRIFLF ADLMPAGIGS SNASVGSGFK EVNGKKYLKL RWHKDAGRAY DYTIREKGVI YNDATNQPTE FRVDGEYNLY QHDTNLTCKQ YDYNFSGNNL IESKTDVDVN MNIFYKNSVF KAFPTNYLAM RYSDDEGASW SDLDIVSSFK PEVSKFLVVG PGIGKQISTG ENAGRLLVPL YSKSSAELGF MYSDDHGDNW TYVEADNLTG GATAEAQIVE MPDGSLKTYL RTGSNCIAEV TSIDGGETWS DRVPLQGIST TSYGTQLSVI NYSQPIDGKP AIILSSPNAT NGRKNGKIWI GLVNDTGNTG IDKYSVEWKY SYAVDTPQMG YSYSCLAELP DGQVGLLYEK YDSWSRNELH LKDILKFEKY SISELTGQAS GN //