NANH_MICVI
ID NANH_MICVI Reviewed; 647 AA.
AC Q02834;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sialidase;
DE EC=3.2.1.18;
DE AltName: Full=Neuraminidase;
DE Flags: Precursor;
GN Name=nedA;
OS Micromonospora viridifaciens.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1881;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-647.
RC STRAIN=ATCC 31146 / DSM 43909 / BCRC 13409 / JCM 3267 / NBRC 101887 / FD
RC 23988;
RX PubMed=1400240; DOI=10.1128/jb.174.21.6896-6903.1992;
RA Sakurada K., Ohta T., Hasegawa M.;
RT "Cloning, expression, and characterization of the Micromonospora
RT viridifaciens neuraminidase gene in Streptomyces lividans.";
RL J. Bacteriol. 174:6896-6903(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC STRAIN=ATCC 31146 / DSM 43909 / BCRC 13409 / JCM 3267 / NBRC 101887 / FD
RC 23988;
RX PubMed=8591030; DOI=10.1016/s0969-2126(01)00255-6;
RA Gaskell A., Crenell S., Taylor G.;
RT "The three domains of a bacterial sialidase: a beta-propeller, an
RT immunoglobulin module and a galactose-binding jelly-roll.";
RL Structure 3:1197-1205(1995).
CC -!- FUNCTION: To release sialic acids for use as carbon and energy sources
CC for this non-pathogenic bacterium while in pathogenic microorganisms,
CC sialidases have been suggested to be pathogenic factors.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By N-acetylneuraminic acid, colominic acid, and sialic acid.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; D01045; BAA00852.1; -; Genomic_DNA.
DR PIR; A45244; A45244.
DR PDB; 1EUR; X-ray; 1.82 A; A=43-407.
DR PDB; 1EUS; X-ray; 2.00 A; A=43-407.
DR PDB; 1EUT; X-ray; 2.50 A; A=43-647.
DR PDB; 1EUU; X-ray; 2.50 A; A=43-647.
DR PDB; 1W8N; X-ray; 2.10 A; A=47-647.
DR PDB; 1W8O; X-ray; 1.70 A; A=47-647.
DR PDB; 1WCQ; X-ray; 2.10 A; A/B/C=47-647.
DR PDB; 2BER; X-ray; 1.80 A; A=47-647.
DR PDB; 2BZD; X-ray; 2.00 A; A/B/C=47-647.
DR PDB; 4J9T; X-ray; 1.40 A; A=47-407.
DR PDBsum; 1EUR; -.
DR PDBsum; 1EUS; -.
DR PDBsum; 1EUT; -.
DR PDBsum; 1EUU; -.
DR PDBsum; 1W8N; -.
DR PDBsum; 1W8O; -.
DR PDBsum; 1WCQ; -.
DR PDBsum; 2BER; -.
DR PDBsum; 2BZD; -.
DR PDBsum; 4J9T; -.
DR AlphaFoldDB; Q02834; -.
DR SMR; Q02834; -.
DR DrugBank; DB03991; 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.
DR DrugBank; DB04465; Lactose.
DR DrugBank; DB04265; N-acetyl-beta-neuraminic acid.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR PRIDE; Q02834; -.
DR BRENDA; 3.2.1.18; 7474.
DR SABIO-RK; Q02834; -.
DR EvolutionaryTrace; Q02834; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR10628; PTHR10628; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR SMART; SM00231; FA58C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:1400240"
FT CHAIN 38..647
FT /note="Sialidase"
FT /id="PRO_0000012032"
FT REPEAT 102..113
FT /note="BNR 1"
FT REPEAT 175..186
FT /note="BNR 2"
FT REPEAT 239..250
FT /note="BNR 3"
FT REPEAT 287..298
FT /note="BNR 4"
FT REPEAT 348..359
FT /note="BNR 5"
FT DOMAIN 496..646
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 370
FT /note="Nucleophile"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1W8N"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2BZD"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:4J9T"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:4J9T"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4J9T"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4J9T"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:4J9T"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 339..352
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:4J9T"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:4J9T"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 462..470
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 478..488
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 491..503
FT /evidence="ECO:0007829|PDB:1W8O"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:1W8O"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1EUT"
FT STRAND 552..571
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:2BZD"
FT STRAND 582..593
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 595..602
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 610..626
FT /evidence="ECO:0007829|PDB:1W8O"
FT STRAND 637..645
FT /evidence="ECO:0007829|PDB:1W8O"
SQ SEQUENCE 647 AA; 68830 MW; DCC1FE5BC935B8AD CRC64;
MTANPYLRRL PRRRAVSFLL APALAAATVA GASPAQAIAG APVPPGGEPL YTEQDLAVNG
REGFPNYRIP ALTVTPDGDL LASYDGRPTG IDAPGPNSIL QRRSTDGGRT WGEQQVVSAG
QTTAPIKGFS DPSYLVDRET GTIFNFHVYS QRQGFAGSRP GTDPADPNVL HANVATSTDG
GLTWSHRTIT ADITPDPGWR SRFAASGEGI QLRYGPHAGR LIQQYTIINA AGAFQAVSVY
SDDHGRTWRA GEAVGVGMDE NKTVELSDGR VLLNSRDSAR SGYRKVAVST DGGHSYGPVT
IDRDLPDPTN NASIIRAFPD APAGSARAKV LLFSNAASQT SRSQGTIRMS CDDGQTWPVS
KVFQPGSMSY STLTALPDGT YGLLYEPGTG IRYANFNLAW LGGICAPFTI PDVALEPGQQ
VTVPVAVTNQ SGIAVPKPSL QLDASPDWQV QGSVEPLMPG RQAKGQVTIT VPAGTTPGRY
RVGATLRTSA GNASTTFTVT VGLLDQARMS IADVDSEETA REDGRASNVI DGNPSTFWHT
EWSRADAPGY PHRISLDLGG THTISGLQYT RRQNSANEQV ADYEIYTSLN GTTWDGPVAS
GRFTTSLAPQ RAVFPARDAR YIRLVALSEQ TGHKYAAVAE LEVEGQR
