Reviewed, UniProtKB/Swiss-Prot P70714 (CYSQ_ACTAC)

Names and origin

Protein names

Recommended name:
    3'(2'),5'-bisphosphate nucleotidase cysQ
    EC=3.1.3.7
Alternative name(s):
    3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
    3'-phosphoadenosine 5'-phosphate phosphatase
      Short name=PAP phosphatase
    DPNPase

Gene names

Name:

cysQ

Organism

Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans)

Taxonomic identifier

714 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Aggregatibacter

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. May also convert adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium By similarity.
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 269	269	3'(2'),5'-bisphosphate nucleotidase cysQ		PRO_0000142547
Sites
	Metal binding	69	1	Magnesium 1 By similarity
	Metal binding	89	1	Magnesium 1 By similarity
	Metal binding	89	1	Magnesium 2 By similarity
	Metal binding	91	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	92	1	Magnesium 2 By similarity
	Metal binding	216	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P70714-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 5E4232ED8021D729	FASTA	269	30,233
	10 20 30 40 50 60 MPILTTHLLQ DVIEIAQQAG EHLRCFYQRS VTVRMKEDNT PVTEADLFVS QFLTEKLTAL 70 80 90 100 110 120 TPQIPILSEE NCHIPLTERQ TWRSYWLIDP LDGTQQFINR TGQFSVLVSL VKDHQPVLGV 130 140 150 160 170 180 IHAPMLGSTY YAMQGFGAYK HHDGQHLKLA FHDIQADNAL RIAVGSAAAA EKVRSILNKN 190 200 210 220 230 240 LAYEFHICGS SGLKSTLVAD GVCDCYIRLG CTGEWDTAAS EILLAEMGGI IFDLNYQPLT 250 260 YNKRESFVNP NFVMGITQDF PWDKIFHSN

References

[1]

"The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA." Yoshida Y., Nakano Y., Yamashita Y., Koga T. Biochem. Biophys. Res. Commun. 230:220-225(1997) [PubMed: 9020051] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43718 / FDC Y4 / Serotype b.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D88189 Genomic DNA. Translation: BAA13553.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR006240. Bisphos_bac. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
ProDom	PD023420. Inositol_P. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01331. bisphos_cysQ. 1 hit.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSQ_ACTAC

Accession

Primary (citable) accession number: P70714

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 48 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)