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P29767

- NANH_CLOSE

UniProt

P29767 - NANH_CLOSE

Protein

Sialidase

Gene
N/A
Organism
Clostridium septicum
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Sialidases have been suggested to be pathogenic factors in microbial infections.

    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 sitei396 – 3961SubstrateBy similarity
    Active sitei421 – 4211Proton acceptorBy similarity
    Binding sitei688 – 6881SubstrateBy similarity
    Binding sitei873 – 8731SubstrateSequence Analysis
    Active sitei912 – 9121NucleophileBy similarity

    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. carbohydrate metabolic process Source: InterPro
    2. cell adhesion Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    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
    OrganismiClostridium septicum
    Taxonomic identifieri1504 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    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 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 1014988SialidasePRO_0000012031Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP29767.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 186148F5/8 type CPROSITE-ProRule annotationAdd
    BLAST
    Repeati431 – 44212BNR 1Add
    BLAST
    Repeati563 – 57412BNR 2Add
    BLAST
    Repeati627 – 63812BNR 3Add
    BLAST
    Repeati700 – 71112BNR 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 4 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. 2 hits.
    2.60.120.200. 1 hit.
    2.60.120.260. 1 hit.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR008979. Galactose-bd-like.
    IPR004124. Glyco_hydro_33_N.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF02973. Sialidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF50939. SSF50939. 2 hits.
    PROSITEiPS50022. FA58C_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29767-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKKKIMSIL VSAFLITNLS SNIIFADIKE NVYINQYSEG NRSQPIAEKL     50
    VPRSEIQASA TSALTGEGPE KAIDGNTSTL WHTPWAGVDI QINPQSLTLK 100
    LGKTRNISSI CVTPRQEGTN GMITDYKIYS GDDVIAEGKW KSDSSDKYVV 150
    FDNPISTDNI RIEAISTVGD ENNKHASIAE VEVYELADTP VKLAESNNKV 200
    INNGNGGNYE GDISEISLLE EGTAIIRFTN NGSSLFSISN NERTNEHFHV 250
    YINGGAIGYE LRKQSGNLAT GSVNKALNAG INTIAFKAEK GKGYSIYLNG 300
    EKILTSSSIT ANFLSTLEGL NTLSLGKTDR PSGSNEYNFT GEIDFFELYS 350
    KPLADRYLKE RTGETTSKDL PFPEGAVKTE PVDIFTPGEL GSNNFRIPAL 400
    YTTKDGTVLA SIDVRKGGGH DAPNNIDTGI KRSTDGGVTW DEGKIILDYP 450
    GASSAIDTSL LQDDETGRIF LIVTHFAEGY GFGNSKTGSG YVEIEGKRYL 500
    KLLGANDTIY TVREGVVYDS NGEATNYTVD NNNELYENGN RIGNVLLSNS 550
    PLKVMGTSFL SLIYSDDDGQ TWSDPIDLNK EVKTDWMRFL GTGPGKGHQI 600
    KTGRYAGRLL FPVYLTNASG FQSSAVIYSD DNGATWNIGE TATDGRLMDN 650
    GDRASAETIT TNTSGGVGQL TECQVVEMPN GQLKMFMRNT GGNSGRVRIA 700
    TSFDGGATWE DDVVRDENIK EPYCQLSVIN YSQKIDGKDA IIFAIPDANY 750
    PNRVNGTVRV GLITENGSYE NGEPRYDIEW RYNKVVAPGT YGYSCLSEMP 800
    NGEIGLFYEG RGSRQMSFTR MNIDYLKADL LQDVPAANIK SYTTNSENNI 850
    YDPGDKISLN VTFDQTVSLI GDRTITADIG GKEVLLTLAN SKGGSEYTFE 900
    GTVPADISNG NYTITIKGKS GLKIVNVVNK VTDITEDRNT GLNVQVGEEV 950
    QSVDKTLLQD LVDSTSNLIK EDYTEESWIL YEKALEVANK FLVNEIAVQE 1000
    EVDAAKPTLE NAYK 1014
    Length:1,014
    Mass (Da):110,653
    Last modified:April 1, 1993 - v1
    Checksum:iC4F49233473A2FAD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63266 Genomic DNA. Translation: CAA44916.1.
    PIRiS15994. NMCLSS.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63266 Genomic DNA. Translation: CAA44916.1 .
    PIRi S15994. NMCLSS.

    3D structure databases

    ProteinModelPortali P29767.
    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...

    Family and domain databases

    Gene3Di 2.120.10.10. 2 hits.
    2.60.120.200. 1 hit.
    2.60.120.260. 1 hit.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR008979. Galactose-bd-like.
    IPR004124. Glyco_hydro_33_N.
    IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    Pfami PF00754. F5_F8_type_C. 1 hit.
    PF02973. Sialidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    SSF50939. SSF50939. 2 hits.
    PROSITEi PS50022. FA58C_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins."
      Rothe B., Rothe B., Roggentin P., Schauer R.
      Mol. Gen. Genet. 226:190-197(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NC 0054714.

    Entry informationi

    Entry nameiNANH_CLOSE
    AccessioniPrimary (citable) accession number: P29767
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3