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

Names and origin

Protein names

Recommended name:
    5'-nucleotidase
    EC=3.1.3.5

Gene names

Name:	nutA
Ordered Locus Names:	VP0748

Organism

Vibrio parahaemolyticus [Complete proteome] [HAMAP]

Taxonomic identifier

670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	560 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.
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.

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 – 560	539	5'-nucleotidase		PRO_0000000029
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
Experimental info
	Sequence conflict	198	1	V → A in CAA40882. Ref.1
	Sequence conflict	198	1	V → A in BAA00756. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22848-1 [UniParc]. Last modified April 4, 2003. Version 2. Checksum: F82E6B4095403D05	FASTA	560	62,175
	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

References

	« Hide 'large scale' referencesShow '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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57711 Genomic DNA. Translation: CAA40882.1. D00910 Genomic DNA. Translation: BAA00756.1. BA000031 Genomic DNA. Translation: BAC59011.1.
PIR	JX0153.
RefSeq	NP_797127.1.
3D structure databases
SMR	P22848. Positions 30-553.
ModBase	Search...
Genome annotation databases
GeneID	1188243.
GenomeReviews	Gene locus VP0748 in contig BA000031_GR.
KEGG	vpa:VP0748.
NMPDR	fig|223926.1.peg.748.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG534106.
OMA	CAPDRQN.
Enzyme and pathway databases
BioCyc	VPAR223926:VP0748-MONOMER.
BRENDA	3.1.3.5. 3063.
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_VIBPA

Accession

Primary (citable) accession number: P22848

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	April 4, 2003
Last modified:	January 19, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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