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Protein

5'-nucleotidase

Gene

nutA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Degradation of extracellular 5'-nucleotides for nutritional needs.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • chlorideBy similarityNote: Chloride.By similarity
  • Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Divalent metal cation 1By similarity1
Metal bindingi47Divalent metal cation 1By similarity1
Metal bindingi88Divalent metal cation 1By similarity1
Metal bindingi88Divalent metal cation 2By similarity1
Metal bindingi120Divalent metal cation 2By similarity1
Sitei121Transition state stabilizerBy similarity1
Sitei124Transition state stabilizerBy similarity1
Metal bindingi221Divalent metal cation 2By similarity1
Metal bindingi256Divalent metal cation 2By similarity1
Metal bindingi258Divalent metal cation 1By similarity1
Binding sitei432SubstrateBy similarity1

GO - Molecular functioni

  • 5'-nucleotidase activity Source: TIGR
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • nucleotide catabolic process Source: InterPro
  • nucleotide-sugar metabolic process Source: TIGR

Keywordsi

Molecular functionHydrolase
LigandMagnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciVCHO:VC2174-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-nucleotidase (EC:3.1.3.5)
Gene namesi
Name:nutA
Ordered Locus Names:VC_2174
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cell outer membrane By similarity; Lipid-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21PROSITE-ProRule annotationAdd BLAST21
ChainiPRO_000000002822 – 5535'-nucleotidaseAdd BLAST532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi22N-palmitoyl cysteineCurated1
Lipidationi22S-diacylglycerol cysteineCurated1

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi243277.VC2174.

Structurei

3D structure databases

ProteinModelPortaliQ9KQ30.
SMRiQ9KQ30.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni501 – 507Substrate bindingBy similarity7

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CGH. Bacteria.
COG0737. LUCA.
KOiK11751.
OMAiCRFQECN.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiView protein in InterPro
IPR008334. 5'-Nucleotdase_C.
IPR036907. 5'-Nucleotdase_C_sf.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiView protein in Pfam
PF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiView protein in PROSITE
PS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9KQ30-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQGLILKSV LSAAIIASLA GCATAPAQQW EADKTYKLTI LHTNDHHGRF
60 70 80 90 100
WQNQYGEYGM AARKTLIDQL RADIEAQGGS VLLLSGGDIN TGVPESDLQD
110 120 130 140 150
AEPDFKGMSK IGYDAMALGN HEFDNPLEVL FKQKEWANFP MLSANIYDKA
160 170 180 190 200
TGKRLFEPYH IFDKQGIKIA VIGLTTEDTA KIGNPEYIGG IDFRDPKEEA
210 220 230 240 250
KKVIAELKKK EKPDLIIAVT HMGHYQNGEH GVNAPGDVAL ARYLPAGELD
260 270 280 290 300
MIVGGHSQEP VCMEGPNLVK KNFKPGDECK PDIQNGTYIV QAYEWGKYVG
310 320 330 340 350
RADYEFRNGE LNMVSYNLIP VNLKKKVEVN GETQRVFATS EIKEDSAMLE
360 370 380 390 400
FLRPFQEKGQ EQLSIKIAHS NGKLEGDRNV VRFEQTNLGR MIAMAHMQRA
410 420 430 440 450
KADFAVMNSG GVRDSIQAGD ITYKDVLKVQ PFGNIVSYVD MNGQEVLDYL
460 470 480 490 500
NVVATKPVDS GAYAQFAGIS MTVADGKVSN VVIGGKQLRL DATYRFTVPS
510 520 530 540 550
FNAAGGDGYP KITDHPGYVN TGFVDAEVLK DYLEANSPID VNRFAPAGEI

VYR
Length:553
Mass (Da):60,903
Last modified:October 1, 2000 - v1
Checksum:i5AA621C27526B311
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95319.1.
PIRiE82108.
RefSeqiNP_231805.1. NC_002505.1.
WP_000809002.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95319; AAF95319; VC_2174.
GeneIDi2613310.
KEGGivch:VC2174.
PATRICifig|243277.26.peg.2072.

Similar proteinsi

Entry informationi

Entry namei5NTD_VIBCH
AccessioniPrimary (citable) accession number: Q9KQ30
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: October 25, 2017
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families