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Q04830

- ENAN_BPK1F

UniProt

Q04830 - ENAN_BPK1F

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Protein

Endo-N-acetylneuraminidase

Gene
N/A
Organism
Enterobacteria phage K1F (Bacteriophage K1F)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Responsible for initial absorption of the phage to the host bacterium. Degradation of the alpha-2,8-linked polysialic acid K1 capsule.

Catalytic activityi

Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.

GO - Molecular functioni

  1. endo-alpha-(2,8)-sialidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.129. 716.

Protein family/group databases

CAZyiGH58. Glycoside Hydrolase Family 58.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-N-acetylneuraminidase (EC:3.2.1.129)
Short name:
Endo-N
Alternative name(s):
Endosialidase
G102
OrganismiEnterobacteria phage K1F (Bacteriophage K1F)
Taxonomic identifieri344021 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostiEscherichia coli [TaxID: 562]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host1 Publication
Chaini2 – 920919Endo-N-acetylneuraminidasePRO_0000057709Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
920
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi249 – 2535Combined sources
Helixi255 – 26410Combined sources
Beta strandi277 – 2793Combined sources
Helixi286 – 2883Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi311 – 3188Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi339 – 35214Combined sources
Beta strandi356 – 3649Combined sources
Beta strandi373 – 3764Combined sources
Turni380 – 3845Combined sources
Beta strandi385 – 3884Combined sources
Beta strandi392 – 3954Combined sources
Beta strandi398 – 40710Combined sources
Turni408 – 4103Combined sources
Beta strandi413 – 42210Combined sources
Beta strandi426 – 4316Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi441 – 4455Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi469 – 4724Combined sources
Beta strandi475 – 4784Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi500 – 5056Combined sources
Beta strandi513 – 5164Combined sources
Beta strandi524 – 5318Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi537 – 5437Combined sources
Beta strandi545 – 5484Combined sources
Beta strandi550 – 5567Combined sources
Turni557 – 5615Combined sources
Beta strandi567 – 5704Combined sources
Helixi573 – 5753Combined sources
Beta strandi579 – 5879Combined sources
Beta strandi590 – 5989Combined sources
Beta strandi606 – 6127Combined sources
Beta strandi618 – 6214Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi639 – 6457Combined sources
Beta strandi667 – 6748Combined sources
Turni675 – 6773Combined sources
Beta strandi686 – 6905Combined sources
Beta strandi696 – 6983Combined sources
Beta strandi702 – 7109Combined sources
Beta strandi713 – 7219Combined sources
Turni728 – 7347Combined sources
Beta strandi746 – 7538Combined sources
Beta strandi772 – 7743Combined sources
Beta strandi784 – 7863Combined sources
Beta strandi790 – 7923Combined sources
Beta strandi796 – 8038Combined sources
Turni808 – 8114Combined sources
Beta strandi812 – 8176Combined sources
Beta strandi819 – 8268Combined sources
Helixi833 – 8353Combined sources
Beta strandi837 – 84711Combined sources
Helixi848 – 8503Combined sources
Beta strandi853 – 8575Combined sources
Beta strandi861 – 8633Combined sources
Beta strandi867 – 8704Combined sources
Beta strandi872 – 8798Combined sources
Beta strandi884 – 8896Combined sources
Beta strandi891 – 8933Combined sources
Beta strandi901 – 9055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]
3GVJX-ray1.48A246-910[»]
3GVKX-ray1.84A/B/C246-910[»]
3GVLX-ray1.41A246-910[»]
3GW6X-ray2.60A/B/C/D/E/F790-913[»]
3JU4X-ray0.98A246-910[»]
ProteinModelPortaliQ04830.
SMRiQ04830. Positions 246-910.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati360 – 37112BNR 1Add
BLAST
Repeati496 – 5038BNR 2
Repeati608 – 61912BNR 3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 21619Gly-rich (hinge)Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 58 family.Curated
Contains 3 BNR repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProiIPR023366. ATPase_asu-like.
IPR024427. Endosialidase_beta_barrel.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C_dom.
IPR024429. Endosialidase_N-extension.
IPR001724. Glycl_Hydrolase_58.
IPR005604. Phage_T7_tail_fibre.
IPR011040. Sialidases.
[Graphical view]
PfamiPF12195. End_beta_barrel. 1 hit.
PF12217. End_beta_propel. 1 hit.
PF12218. End_N_terminal. 1 hit.
PF12219. End_tail_spike. 1 hit.
PF03906. Phage_T7_tail. 1 hit.
[Graphical view]
PRINTSiPR00849. GLHYDRLASE58.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q04830-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF
60 70 80 90 100
LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA
110 120 130 140 150
IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG
160 170 180 190 200
YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG
210 220 230 240 250
IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG
260 270 280 290 300
VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP
310 320 330 340 350
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH
360 370 380 390 400
GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF
410 420 430 440 450
AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
460 470 480 490 500
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN
510 520 530 540 550
WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE
560 570 580 590 600
VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG
610 620 630 640 650
DRLGSSLHRS RDIGQTWESL RFPHNVHRTT LPFAKVGDDL IMFGSERAEN
660 670 680 690 700
EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS
710 720 730 740 750
GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY
760 770 780 790 800
KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH
810 820 830 840 850
VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT
860 870 880 890 900
GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT
910 920
AYLGSNPIVT SNGGGGKQSR
Length:920
Mass (Da):102,013
Last modified:January 23, 2007 - v3
Checksum:i62B77613F55884B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63657 Unassigned DNA. Translation: AAC37340.1.
PIRiA36887.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63657 Unassigned DNA. Translation: AAC37340.1 .
PIRi A36887.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V0E X-ray 1.90 A/B/C/D/E/F 246-910 [» ]
1V0F X-ray 2.55 A/B/C/D/E/F 246-910 [» ]
3GVJ X-ray 1.48 A 246-910 [» ]
3GVK X-ray 1.84 A/B/C 246-910 [» ]
3GVL X-ray 1.41 A 246-910 [» ]
3GW6 X-ray 2.60 A/B/C/D/E/F 790-913 [» ]
3JU4 X-ray 0.98 A 246-910 [» ]
ProteinModelPortali Q04830.
SMRi Q04830. Positions 246-910.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH58. Glycoside Hydrolase Family 58.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.129. 716.

Miscellaneous databases

EvolutionaryTracei Q04830.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProi IPR023366. ATPase_asu-like.
IPR024427. Endosialidase_beta_barrel.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C_dom.
IPR024429. Endosialidase_N-extension.
IPR001724. Glycl_Hydrolase_58.
IPR005604. Phage_T7_tail_fibre.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF12195. End_beta_barrel. 1 hit.
PF12217. End_beta_propel. 1 hit.
PF12218. End_N_terminal. 1 hit.
PF12219. End_tail_spike. 1 hit.
PF03906. Phage_T7_tail. 1 hit.
[Graphical view ]
PRINTSi PR00849. GLHYDRLASE58.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete nucleotide sequence of the bacteriophage K1F tail gene encoding endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in bacteriophage PK1E."
    Petter J.G., Vimr E.R.
    J. Bacteriol. 175:4354-4363(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-31 AND 917-920.

Entry informationi

Entry nameiENAN_BPK1F
AccessioniPrimary (citable) accession number: Q04830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral 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