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Q02834

- NANH_MICVI

UniProt

Q02834 - NANH_MICVI

Protein

Sialidase

Gene

nedA

Organism
Micromonospora viridifaciens
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.

    Catalytic activityi

    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei68 – 681SubstrateBy similarity
    Active sitei92 – 921Proton acceptorBy similarity
    Active sitei260 – 2601NucleophileSequence Analysis
    Binding sitei276 – 2761SubstrateBy similarity
    Active sitei370 – 3701Nucleophile

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell adhesion Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    SABIO-RKQ02834.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase (EC:3.2.1.18)
    Alternative name(s):
    Neuraminidase
    Gene namesi
    Name:nedA
    OrganismiMicromonospora viridifaciens
    Taxonomic identifieri1881 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeMicromonospora

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 37371 PublicationAdd
    BLAST
    Chaini38 – 647610SialidasePRO_0000012032Add
    BLAST

    Expressioni

    Inductioni

    By N-acetylneuraminic acid, colominic acid, and sialic acid.

    Structurei

    Secondary structure

    1
    647
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi51 – 588
    Beta strandi61 – 633
    Beta strandi65 – 7410
    Beta strandi80 – 878
    Beta strandi98 – 1069
    Beta strandi107 – 1093
    Beta strandi115 – 1184
    Beta strandi123 – 1253
    Beta strandi127 – 13610
    Turni138 – 1403
    Beta strandi143 – 15210
    Turni155 – 1573
    Beta strandi171 – 1799
    Beta strandi185 – 1884
    Helixi190 – 1934
    Beta strandi201 – 2044
    Beta strandi206 – 2083
    Turni216 – 2194
    Beta strandi221 – 2288
    Beta strandi234 – 24310
    Beta strandi260 – 2656
    Beta strandi271 – 2755
    Beta strandi282 – 29110
    Beta strandi300 – 3067
    Beta strandi313 – 3186
    Helixi327 – 3293
    Beta strandi331 – 3366
    Beta strandi339 – 35214
    Beta strandi359 – 3679
    Beta strandi371 – 3755
    Beta strandi381 – 3855
    Beta strandi388 – 3969
    Helixi398 – 4014
    Beta strandi413 – 4153
    Beta strandi420 – 4289
    Beta strandi431 – 4333
    Beta strandi435 – 4373
    Beta strandi439 – 4435
    Beta strandi448 – 4547
    Beta strandi462 – 4709
    Beta strandi478 – 48811
    Beta strandi491 – 50313
    Helixi506 – 5083
    Beta strandi510 – 5156
    Beta strandi520 – 5223
    Helixi526 – 5305
    Beta strandi543 – 5453
    Beta strandi552 – 57120
    Beta strandi576 – 5783
    Beta strandi582 – 59312
    Beta strandi595 – 6028
    Beta strandi610 – 62617
    Beta strandi637 – 6459

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EURX-ray1.82A43-407[»]
    1EUSX-ray2.00A43-407[»]
    1EUTX-ray2.50A43-647[»]
    1EUUX-ray2.50A43-647[»]
    1W8NX-ray2.10A47-647[»]
    1W8OX-ray1.70A47-647[»]
    1WCQX-ray2.10A/B/C47-647[»]
    2BERX-ray1.80A47-647[»]
    2BZDX-ray2.00A/B/C47-647[»]
    4J9TX-ray1.40A47-407[»]
    ProteinModelPortaliQ02834.
    SMRiQ02834. Positions 47-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02834.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati102 – 11312BNR 1Add
    BLAST
    Repeati175 – 18612BNR 2Add
    BLAST
    Repeati239 – 25012BNR 3Add
    BLAST
    Repeati287 – 29812BNR 4Add
    BLAST
    Repeati348 – 35912BNR 5Add
    BLAST
    Domaini496 – 646151F5/8 type CPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 5 BNR repeats.Curated
    Contains 1 F5/8 type C domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    InterProiIPR018905. A-galactase_NEW3.
    IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    IPR006311. TAT_signal.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF10633. NPCBM_assoc. 1 hit.
    [Graphical view]
    SMARTiSM00231. FA58C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF50939. SSF50939. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS50022. FA58C_3. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q02834-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTANPYLRRL PRRRAVSFLL APALAAATVA GASPAQAIAG APVPPGGEPL    50
    YTEQDLAVNG REGFPNYRIP ALTVTPDGDL LASYDGRPTG IDAPGPNSIL 100
    QRRSTDGGRT WGEQQVVSAG QTTAPIKGFS DPSYLVDRET GTIFNFHVYS 150
    QRQGFAGSRP GTDPADPNVL HANVATSTDG GLTWSHRTIT ADITPDPGWR 200
    SRFAASGEGI QLRYGPHAGR LIQQYTIINA AGAFQAVSVY SDDHGRTWRA 250
    GEAVGVGMDE NKTVELSDGR VLLNSRDSAR SGYRKVAVST DGGHSYGPVT 300
    IDRDLPDPTN NASIIRAFPD APAGSARAKV LLFSNAASQT SRSQGTIRMS 350
    CDDGQTWPVS KVFQPGSMSY STLTALPDGT YGLLYEPGTG IRYANFNLAW 400
    LGGICAPFTI PDVALEPGQQ VTVPVAVTNQ SGIAVPKPSL QLDASPDWQV 450
    QGSVEPLMPG RQAKGQVTIT VPAGTTPGRY RVGATLRTSA GNASTTFTVT 500
    VGLLDQARMS IADVDSEETA REDGRASNVI DGNPSTFWHT EWSRADAPGY 550
    PHRISLDLGG THTISGLQYT RRQNSANEQV ADYEIYTSLN GTTWDGPVAS 600
    GRFTTSLAPQ RAVFPARDAR YIRLVALSEQ TGHKYAAVAE LEVEGQR 647
    Length:647
    Mass (Da):68,830
    Last modified:October 1, 1994 - v1
    Checksum:iDCC1FE5BC935B8AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D01045 Genomic DNA. Translation: BAA00852.1.
    PIRiA45244.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D01045 Genomic DNA. Translation: BAA00852.1 .
    PIRi A45244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EUR X-ray 1.82 A 43-407 [» ]
    1EUS X-ray 2.00 A 43-407 [» ]
    1EUT X-ray 2.50 A 43-647 [» ]
    1EUU X-ray 2.50 A 43-647 [» ]
    1W8N X-ray 2.10 A 47-647 [» ]
    1W8O X-ray 1.70 A 47-647 [» ]
    1WCQ X-ray 2.10 A/B/C 47-647 [» ]
    2BER X-ray 1.80 A 47-647 [» ]
    2BZD X-ray 2.00 A/B/C 47-647 [» ]
    4J9T X-ray 1.40 A 47-407 [» ]
    ProteinModelPortali Q02834.
    SMRi Q02834. Positions 47-647.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM32. Carbohydrate-Binding Module Family 32.
    GH33. Glycoside Hydrolase Family 33.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q02834.

    Miscellaneous databases

    EvolutionaryTracei Q02834.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    InterProi IPR018905. A-galactase_NEW3.
    IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    IPR006311. TAT_signal.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    Pfami PF00754. F5_F8_type_C. 1 hit.
    PF10633. NPCBM_assoc. 1 hit.
    [Graphical view ]
    SMARTi SM00231. FA58C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF50939. SSF50939. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS50022. FA58C_3. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of the Micromonospora viridifaciens neuraminidase gene in Streptomyces lividans."
      Sakurada K., Ohta T., Hasegawa M.
      J. Bacteriol. 174:6896-6903(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-647.
      Strain: ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267.
    2. "The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll."
      Gaskell A., Crenell S., Taylor G.
      Structure 3:1197-1205(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
      Strain: ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267.

    Entry informationi

    Entry nameiNANH_MICVI
    AccessioniPrimary (citable) accession number: Q02834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3