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Reviewed, UniProtKB/Swiss-Prot P22848 (5NTD_VIBPA)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    5'-nucleotidase
    EC=3.1.3.5
Gene names
Name: nutA
Ordered Locus Names: VP0748
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

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Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Degradation of extracellular 5'-nucleotides for nutritional needs.

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Chloride.

Magnesium.

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the 5'-nucleotidase family.

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Ontologies

Keywords
   Cellular componentCell membrane
Cell outer membrane
Membrane
   DomainSignal
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMLipoprotein
Palmitate
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function5'-nucleotidase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 5605395'-nucleotidase
PRO_0000000029

Regions

Region501 – 5077Substrate binding By similarity

Sites

Metal binding451Divalent metal cation 1 By similarity
Metal binding471Divalent metal cation 1 By similarity
Metal binding881Divalent metal cation 1 By similarity
Metal binding881Divalent metal cation 2 By similarity
Metal binding1201Divalent metal cation 2 By similarity
Metal binding2211Divalent metal cation 2 By similarity
Metal binding2561Divalent metal cation 2 By similarity
Metal binding2581Divalent metal cation 1 By similarity
Binding site4321Substrate By similarity
Site1211Transition state stabilizer By similarity
Site1241Transition state stabilizer By similarity

Amino acid modifications

Lipidation221N-palmitoyl cysteine Probable
Lipidation221S-diacylglycerol cysteine Probable

Experimental info

Sequence conflict1981V → A in CAA40882. Ref.1
Sequence conflict1981V → A in BAA00756. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P22848-1 [UniParc].

Last modified April 4, 2003. Version 2.
Checksum: F82E6B4095403D05

FASTA56062,175
        10         20         30         40         50         60 
MNQRLIIKTA LSAAILASLA GCASQPAHEW NADTTYKLTV LHTNDHHGRF WQNKHGEYGM 

        70         80         90        100        110        120 
AARKTLIDDL RDEIQAEGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN 

       130        140        150        160        170        180 
HEFDNPLDVL FKQQDWANFP MLSANIYDKK TGKRLFQPYA MFNKQGIKIA VIGLTTEDTA 

       190        200        210        220        230        240 
KLGNPEFIGQ VDFRDPKVEA KELIAELKKT ENPDLIFAVT HMGHYENGNR GINAPGDVAL 

       250        260        270        280        290        300 
ARYLNEGDLD MIVGGHSQEP VCMEGPNVIK KNFKPGDECQ PDQQNGTYIV QAHEWGKYVG 

       310        320        330        340        350        360 
RADYEFRNGE LSMVSYDLIP VNLKKKINVD GQSQRVFVQD EITQDKAMLD FLRPFQEKGQ 

       370        380        390        400        410        420 
SQLNVKIAES NGKLEGDRDV VRFQQTNLGR LIATAHMERA KADFAVMNSG GVRDSIEAGD 

       430        440        450        460        470        480 
ITYKDVLTVQ PFGNMVSYVD MSGQEVLDYL NIVATKPVDS GAYAQFAGIS MRIENDKVTN 

       490        500        510        520        530        540 
VFIGNKQLRL DGRYRFTVPS YNASGGDGYP KIDTHPGYVN TGFTDAEVLK DYLESHSPID 

       550        560 
VNEYAPSGEV MYQTNNVVNQ

« Hide

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References

« Hide 'large scale' references
[1]"Sequence analysis of nutA gene encoding membrane-bound Cl(-)-dependent 5'-nucleotidase of Vibrio parahaemolyticus."
Tamao Y., Noguchi K., Sakai-Tomita Y., Hama H., Shimamoto T., Kanazawa H., Tsuda M., Tsuchiya T.
J. Biochem. 109:24-29(1991) [PubMed: 2016269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AQ3334.
[2]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

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Cross-references

Sequence databases

X57711 Genomic DNA. Translation: CAA40882.1.
D00910 Genomic DNA. Translation: BAA00756.1.
BA000031 Genomic DNA. Translation: BAC59011.1.
PIRJX0153.
RefSeqNP_797127.1.

3D structure databases

HSSPHSSP built from PDB template 2USH based on UniProtKB P07024.
ModBaseSearch...

Genome annotation databases

GeneID1188243.
GenomeReviewsGene locus VP0748 in contig BA000031_GR.
KEGGvpa:VP0748.
NMPDRfig|223926.1.peg.748.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP22848.
OMAP22848. VKIKGEP.

Enzyme and pathway databases

BioCycVPAR223926:VP0748-MON.
BRENDA3.1.3.5. 3063.

Family and domain databases

InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase.
IPR004843. M-pesterase.
[Graphical view]
Gene3DG3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHERPTHR11575. 5_nucleotidase. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry name5NTD_VIBPA
AccessionPrimary (citable) accession number: P22848
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: April 4, 2003
Last modified: June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents