Reviewed, UniProtKB/Swiss-Prot Q9KQ30 (5NTD_VIBCH)

Names and origin

Protein names

Recommended name:
    5'-nucleotidase
    EC=3.1.3.5

Gene names

Name:	nutA
Ordered Locus Names:	VC_2174

Organism

Vibrio cholerae [Complete proteome] [HAMAP]

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Degradation of extracellular 5'-nucleotides for nutritional needs By similarity.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Chloride By similarity. Magnesium By similarity.
Subcellular location	Cell outer membrane; Lipid-anchor By similarity.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Lipoprotein Palmitate
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell outer membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	5'-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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 553	532	5'-nucleotidase		PRO_0000000028
Regions
	Region	501 – 507	7	Substrate binding By similarity
Sites
	Metal binding	45	1	Divalent metal cation 1 By similarity
	Metal binding	47	1	Divalent metal cation 1 By similarity
	Metal binding	88	1	Divalent metal cation 1 By similarity
	Metal binding	88	1	Divalent metal cation 2 By similarity
	Metal binding	120	1	Divalent metal cation 2 By similarity
	Metal binding	221	1	Divalent metal cation 2 By similarity
	Metal binding	256	1	Divalent metal cation 2 By similarity
	Metal binding	258	1	Divalent metal cation 1 By similarity
	Binding site	432	1	Substrate By similarity
	Site	121	1	Transition state stabilizer By similarity
	Site	124	1	Transition state stabilizer By similarity
Amino acid modifications
	Lipidation	22	1	N-palmitoyl cysteine Probable
	Lipidation	22	1	S-diacylglycerol cysteine Probable

Sequences

	Sequence		Length	Mass (Da)
	Q9KQ30-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5AA621C27526B311	FASTA	553	60,903
	10 20 30 40 50 60 MKQGLILKSV LSAAIIASLA GCATAPAQQW EADKTYKLTI LHTNDHHGRF WQNQYGEYGM 70 80 90 100 110 120 AARKTLIDQL RADIEAQGGS VLLLSGGDIN TGVPESDLQD AEPDFKGMSK IGYDAMALGN 130 140 150 160 170 180 HEFDNPLEVL FKQKEWANFP MLSANIYDKA TGKRLFEPYH IFDKQGIKIA VIGLTTEDTA 190 200 210 220 230 240 KIGNPEYIGG IDFRDPKEEA KKVIAELKKK EKPDLIIAVT HMGHYQNGEH GVNAPGDVAL 250 260 270 280 290 300 ARYLPAGELD MIVGGHSQEP VCMEGPNLVK KNFKPGDECK PDIQNGTYIV QAYEWGKYVG 310 320 330 340 350 360 RADYEFRNGE LNMVSYNLIP VNLKKKVEVN GETQRVFATS EIKEDSAMLE FLRPFQEKGQ 370 380 390 400 410 420 EQLSIKIAHS NGKLEGDRNV VRFEQTNLGR MIAMAHMQRA KADFAVMNSG GVRDSIQAGD 430 440 450 460 470 480 ITYKDVLKVQ PFGNIVSYVD MNGQEVLDYL NVVATKPVDS GAYAQFAGIS MTVADGKVSN 490 500 510 520 530 540 VVIGGKQLRL DATYRFTVPS FNAAGGDGYP KITDHPGYVN TGFVDAEVLK DYLEANSPID 550 VNRFAPAGEI VYR

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE003852 Genomic DNA. Translation: AAF95319.1.
PIR	E82108.
RefSeq	NP_231805.1.
3D structure databases
HSSP	HSSP built from PDB template 2USH based on UniProtKB P07024.
ModBase	Search...
Genome annotation databases
GeneID	2613310.
GenomeReviews	Gene locus VC_2174 in contig AE003852_GR.
KEGG	vch:VC2174.
TIGR	VC_2174.
Phylogenomic databases
HOGENOM	Q9KQ30.
OMA	QADYVPG.
Enzyme and pathway databases
BRENDA	3.1.3.5. 19019.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. M-pesterase. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. PS51257. PROKAR_LIPOPROTEIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

5NTD_VIBCH

Accession

Primary (citable) accession number: Q9KQ30

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)