NANL_MACDE
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 03-AUG-2022, entry version 112.
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 PRIDE; Q27701; -.
DR EvolutionaryTrace; Q27701; -.
DR GO; GO:0005615; C:extracellular space; 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 Gene3D; 2.40.220.10; -; 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; PTHR10628; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF02973; Sialidase; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50939; SSF50939; 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
