Reviewed, UniProtKB/Swiss-Prot Q59XQ1 (HAL22_CANAL)

Names and origin

Protein names

Recommended name:
    3'(2'),5'-bisphosphate nucleotidase 2
    EC=3.1.3.7
Alternative name(s):
    3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase 2
    DPNPase 2
    Halotolerance protein HAL22

Gene names

Name:	HAL22
Synonyms:	MET221
ORF Names:	CaO19.105, CaO19.7752

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW sulfur metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from electronic annotation. Source: EC inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro magnesium ion 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
	Chain	1 – 358	358	3'(2'),5'-bisphosphate nucleotidase 2		PRO_0000245648
Sites
	Metal binding	77	1	Magnesium 1 By similarity
	Metal binding	141	1	Magnesium 1 By similarity
	Metal binding	141	1	Magnesium 2 By similarity
	Metal binding	143	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	144	1	Magnesium 2 By similarity
	Metal binding	302	1	Magnesium 2 By similarity
Natural variations
	Natural variant	24	1	L → M in allele CaO19.7752.
	Natural variant	81	1	R → Q in allele CaO19.7752.
	Natural variant	87 – 88	2	TG → NS in allele CaO19.7752.
	Natural variant	93	1	M → V in allele CaO19.7752.
	Natural variant	95	1	Q → S in allele CaO19.7752.
	Natural variant	98	1	T → I in allele CaO19.7752.
	Natural variant	119	1	E → K in allele CaO19.7752.
	Natural variant	121 – 122	2	YQ → FE in allele CaO19.7752.
	Natural variant	185	1	E → D in allele CaO19.7752.
	Natural variant	207	1	D → E in allele CaO19.7752.
	Natural variant	227	1	H → Q in allele CaO19.7752.
	Natural variant	229	1	N → D in allele CaO19.7752.
	Natural variant	250	1	A → T in allele CaO19.7752.
	Natural variant	260 – 261	2	SA → PT in allele CaO19.7752.
	Natural variant	293 – 294	2	SD → NE in allele CaO19.7752.
	Natural variant	323	1	S → A in allele CaO19.7752.
	Natural variant	344	1	E → G in allele CaO19.7752.

Sequences

	Sequence		Length	Mass (Da)
	Q59XQ1-1 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: C35D476D10A69599	FASTA	358	38,705
	10 20 30 40 50 60 MSHSTHPYQK ELEVATLAVK RASLLTKQLS DSIVQTAKSG TLTKDDKSPV TIGDFASQAI 70 80 90 100 110 120 INHAIKLNFP NDEIVGEEDS RELQENTGLA DQMLQLITKI QKETSGYNDI VGTLTDKNEV 130 140 150 160 170 180 YQSIDFGNSQ GGSKGRFWAL DPIDGTKGFL RGDQFAVCLA LIEDGKVVLG VIGCPNLSEN 190 200 210 220 230 240 IVSNEEHSGV VGGLYSAVKG VGSFYSDLFK EGAEPLSQQK RIKMQNHTNP SQLKVVEGVE 250 260 270 280 290 300 KGHSSHSTQA EIKAKLGFDS ATVAKQTINL DSQVKYCVLA SGQADIYLRL PVSDTYREKI 310 320 330 340 350 WDHAAGNILI YESGGQVGDV TGSPLNFGNG RTLDSKGVIA ANKEIFDKVI DAVTEVRK

References

[1]

"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACQ01000106 Genomic DNA. Translation: EAK95242.1. Different initiation. AACQ01000112 Genomic DNA. Translation: EAK94942.1. Different initiation.
RefSeq	XP_714039.1. XP_714314.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3644051. 3644292.
KEGG	cal:CaO19.105. cal:CaO19.7752.
Phylogenomic databases
OMA	Q59XQ1. DASFFES.
Enzyme and pathway databases
BRENDA	3.1.3.7. 1124.
Family and domain databases
InterPro	IPR006239. Bisphos_HAL2. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
TIGRFAMs	TIGR01330. bisphos_HAL2. 1 hit.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HAL22_CANAL

Accession

Primary (citable) accession number: Q59XQ1
Secondary accession number(s): Q59WU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 11, 2006
Last modified:	June 16, 2009
This is version 25 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)