Sialidase - Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Sialidase EMBL ABG84247.1

Gene names

Name:	nanJ EMBL ABG84247.1
Ordered Locus Names:	CPF_0532

Organism

Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

195103 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1173 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 fibronectin type-III domain. RuleBase RU000718

Ontologies

Keywords
Ligand	Calcium PDB 2V73 Metal-binding PDB 2V73
Technical term	3D-structure PDB 2V73 PDB 2VO8 Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell adhesion Inferred from electronic annotation. Source: InterPro
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

225

1

Calcium 1 PDB 2V73

Metal binding

226

1

Calcium 1; via carbonyl oxygen PDB 2V73

Metal binding

281

1

Calcium 1; via carbonyl oxygen PDB 2V73

Metal binding

330

1

Calcium 2 PDB 2V73

Metal binding

331

1

Calcium 2; via carbonyl oxygen PDB 2V73

Metal binding

337

1

Calcium 2 PDB 2V73

Sequences

Sequence

Length

Mass (Da)

Tools

Q0TTQ4 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: D5A7CC27735851FE
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FASTA

1,173

128,883

        10         20         30         40         50         60 
MKSKKIIATL VASLVISNMG GYLVKANPNV NHKAVIIEDR QAIIETAIPQ SEMTASATSE 

        70         80         90        100        110        120 
EGQDPASSAI DGNTNTMWHT KWNGSDALPQ SLSVNLGSSR KVSSIAITPR TSGNNGFITK 

       130        140        150        160        170        180 
YEIHAINNGV EALVAEGTWE ENNLVKTVTF DSPIDAEEIK ITAIQGVGGF ASIAELNVYE 

       190        200        210        220        230        240 
IKGEVDEIAN YGNLKITKEE ERVNITGDLE KFSSLEEGTI VTRFNMNDTS IQSLIGLSDG 

       250        260        270        280        290        300 
NKANNYFSLY VSGGKVGYEL RRQEGNGDFN VHHSADVTFN RGINTLALKI EKGIGAKIFL 

       310        320        330        340        350        360 
NGSLVKTVSD PNIKFLNAIN LNSGFIGKTD RANGYNEYLF RGNIDFMNIY DKPVSDNYLL 

       370        380        390        400        410        420 
RKTGETKAPL EDSLLPDDVY KTQPVELFYP GYLESRGYRI PALETTKKGT VLASIDVRNN 

       430        440        450        460        470        480 
GDHDAPNNNI DVGIRRKEVN GEWEEGKVIL DYPGKSAAID TSLMSATIEE NGIEKERIFL 

       490        500        510        520        530        540 
IVTHFPEGYG FPNTEGGSGY REIDGKYYFI LKDAQNNEYT VREDGIVYNS EGNQTDYVMK 

       550        560        570        580        590        600 
NDKTLIQNGE EVGNALLSNS PLKAVGTAHI EMIYSDDDGK TWSEPEDLNP GLKKEWMKFF 

       610        620        630        640        650        660 
GTAPGKGIQI KNGEHKDRLI FPIYYTNQNN FQSSAVIYSD DFGETWKLGE SPIDTASVSS 

       670        680        690        700        710        720 
ETVSSGTQLT ECQVVEMPNG QLKLFMRNTG SYTRIATSFD GGATWHDEVP EDTSLREPYC 

       730        740        750        760        770        780 
QLSVINYSGK INGKDAIIFS NPDASSRVNG SVKVGLINEN GTYDNGEPRY EFDWIYNKTV 

       790        800        810        820        830        840 
KPGSFAYSCL TELPDGNLGL FYEGEGAGRM AYTEFDLNYL KFNASEDSPS ASVQSIEVLD 

       850        860        870        880        890        900 
EDLAYNSGEE VSIKVNFNQL VSIIGDRKIT LDIGGVDVPL NMVNYEGKSS AIFKGTIPEG 

       910        920        930        940        950        960 
INQGNYEIKL KENNTLELNT VYNKVSTFNG LDNTGINVQI GELKTTVGNS TIKVNDEVQV 

       970        980        990       1000       1010       1020 
GSAFEAILGI EGLNGDTEVY SAEYLFEYNA EAFILNEITS FNDSLFVKSK EVEPGKVRIL 

      1030       1040       1050       1060       1070       1080 
VASLGNEIEK DSDLVKVNLT PKISSELEVL GLTTALVGAG DGNTHDLELS SKEVKINEEA 

      1090       1100       1110       1120       1130       1140 
SGEIVVNPVQ NFEIPEINKK NVKLTWNAPI TTEGLEGYVI YKDGKKLSEV PAESTEFVVS 

      1150       1160       1170 
KLNRHTIYNF KVAAKYSNGE LSAKESKTIR TAR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens." Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. Paulsen I.T. Genome Res. 16:1031-1040(2006) [PubMed: 16825665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Structural basis of Clostridium perfringens toxin complex formation." Adams J.J., Gregg K., Bayer E.A., Boraston A.B., Smith S.P. Proc. Natl. Acad. Sci. U.S.A. 105:12194-12199(2008) [PubMed: 18716000] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 939-1081.
[3]	"Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens." Boraston A.B., Ficko-Blean E., Healey M. Biochemistry 46:11352-11360(2007) [PubMed: 17850114] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 181-367 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000246 Genomic DNA. Translation: ABG84247.1.

RefSeq

YP_694986.1. NC_008261.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V73	X-ray	2.20	A/B	181-367	[»]
2VO8	X-ray	1.70	A	939-1081	[»]

ProteinModelPortal

Q0TTQ4.

SMR

Q0TTQ4. Positions 44-180, 185-367, 378-821.

ModBase

Search...

Protein-protein interaction databases

STRING

Q0TTQ4.

Protein family/group databases

CAZy

CBM32. Carbohydrate-Binding Module Family 32.
CBM40. Carbohydrate-Binding Module Family 40.
GH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

4202243.

GenomeReviews

Gene locus CPF_0532 in contig CP000246_GR.

KEGG

cpf:CPF_0532.

PATRIC

19483368. VBICloPer106549_0511.

TIGR

CPF_0532.

Phylogenomic databases

eggNOG

COG4409.

HOGENOM

HBG428587.

OMA

EVDEIAN.

ProtClustDB

CLSK518658.

Family and domain databases

InterPro

IPR002860. BNR_rpt.
IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR004124. Glyco_hydro_33_N.
IPR013783. Ig-like_fold.
IPR011040. Neuraminidase.
IPR021984. Sialidase_penC.
IPR023364. Trans_sialidase_dom3.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
G3DSA:2.40.220.10. G3DSA:2.40.220.10. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.120.10.10. Neuraminidase. 2 hits.

KO

K01186.

Pfam

PF02012. BNR. 3 hits.
PF00754. F5_F8_type_C. 1 hit.
PF00041. fn3. 1 hit.
PF02973. Sialidase. 1 hit.
PF12135. Sialidase_penC. 1 hit.
[Graphical view]

SMART

SM00060. FN3. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF49265. FN_III-like. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF50939. Sialidase. 1 hit.

PROSITE

PS50022. FA58C_3. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q0TTQ4_CLOP1

Accession

Primary (citable) accession number: Q0TTQ4

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	December 14, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)