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P29767

- NANH_CLOSE

UniProt

P29767 - NANH_CLOSE

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Protein

Sialidase

Gene
N/A
Organism
Clostridium septicum
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
IPR013320. ConA-like_dom.
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

        10         20         30         40         50
MNKKKIMSIL VSAFLITNLS SNIIFADIKE NVYINQYSEG NRSQPIAEKL
60 70 80 90 100
VPRSEIQASA TSALTGEGPE KAIDGNTSTL WHTPWAGVDI QINPQSLTLK
110 120 130 140 150
LGKTRNISSI CVTPRQEGTN GMITDYKIYS GDDVIAEGKW KSDSSDKYVV
160 170 180 190 200
FDNPISTDNI RIEAISTVGD ENNKHASIAE VEVYELADTP VKLAESNNKV
210 220 230 240 250
INNGNGGNYE GDISEISLLE EGTAIIRFTN NGSSLFSISN NERTNEHFHV
260 270 280 290 300
YINGGAIGYE LRKQSGNLAT GSVNKALNAG INTIAFKAEK GKGYSIYLNG
310 320 330 340 350
EKILTSSSIT ANFLSTLEGL NTLSLGKTDR PSGSNEYNFT GEIDFFELYS
360 370 380 390 400
KPLADRYLKE RTGETTSKDL PFPEGAVKTE PVDIFTPGEL GSNNFRIPAL
410 420 430 440 450
YTTKDGTVLA SIDVRKGGGH DAPNNIDTGI KRSTDGGVTW DEGKIILDYP
460 470 480 490 500
GASSAIDTSL LQDDETGRIF LIVTHFAEGY GFGNSKTGSG YVEIEGKRYL
510 520 530 540 550
KLLGANDTIY TVREGVVYDS NGEATNYTVD NNNELYENGN RIGNVLLSNS
560 570 580 590 600
PLKVMGTSFL SLIYSDDDGQ TWSDPIDLNK EVKTDWMRFL GTGPGKGHQI
610 620 630 640 650
KTGRYAGRLL FPVYLTNASG FQSSAVIYSD DNGATWNIGE TATDGRLMDN
660 670 680 690 700
GDRASAETIT TNTSGGVGQL TECQVVEMPN GQLKMFMRNT GGNSGRVRIA
710 720 730 740 750
TSFDGGATWE DDVVRDENIK EPYCQLSVIN YSQKIDGKDA IIFAIPDANY
760 770 780 790 800
PNRVNGTVRV GLITENGSYE NGEPRYDIEW RYNKVVAPGT YGYSCLSEMP
810 820 830 840 850
NGEIGLFYEG RGSRQMSFTR MNIDYLKADL LQDVPAANIK SYTTNSENNI
860 870 880 890 900
YDPGDKISLN VTFDQTVSLI GDRTITADIG GKEVLLTLAN SKGGSEYTFE
910 920 930 940 950
GTVPADISNG NYTITIKGKS GLKIVNVVNK VTDITEDRNT GLNVQVGEEV
960 970 980 990 1000
QSVDKTLLQD LVDSTSNLIK EDYTEESWIL YEKALEVANK FLVNEIAVQE
1010
EVDAAKPTLE NAYK
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.
IPR013320. ConA-like_dom.
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 29, 2014
This is version 86 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