Arylsulfatase
Details
- Name
- Arylsulfatase
- Synonyms
- 3.1.6.1
- Aryl-sulfate sulphohydrolase
- AS
- Gene Name
- atsA
- Organism
- Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
- Amino acid sequence
>lcl|BSEQ0019130|Arylsulfatase MSKRPNFLVIVADDLGFSDIGAFGGEIATPNLDALAIAGLRLTDFHTASTCSPTRSMLLT GTDHHIAGIGTMAEALTPELEGKPGYEGHLNERVVALPELLREAGYQTLMAGKWHLGLKP EQTPHARGFERSFSLLPGAANHYGFEPPYDESTPRILKGTPALYVEDERYLDTLPEGFYS SDAFGDKLLQYLKERDQSRPFFAYLPFSAPHWPLQAPREIVEKYRGRYDAGPEALRQERL ARLKELGLVEADVEAHPVLALTREWEALEDEERAKSARAMEVYAAMVERMDWNIGRVVDY LRRQGELDNTFVLFMSDNGAEGALLEAFPKFGPDLLGFLDRHYDNSLENIGRANSYVWYG PRWAQAATAPSRLYKAFTTQGGIRVPALVRYPRLSRQGAISHAFATVMDVTPTLLDLAGV RHPGKRWRGREIAEPRGRSWLGWLSGETEAAHDENTVTGWELFGMRAIRQGDWKAVYLPA PVGPATWQLYDLARDPGEIHDLADSQPGKLAELIEHWKRYVSETGVVEGASPFLVR
- Number of residues
- 536
- Molecular Weight
- 59945.155
- Theoretical pI
- 5.51
- GO Classification
- Functionsarylsulfatase activity / metal ion binding / phosphoric diester hydrolase activityComponentscytoplasm
- General Function
- Phosphoric diester hydrolase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Sulfatase (PF00884)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019131|Arylsulfatase (atsA) ATGAGCAAACGCCCCAACTTCCTGGTGATCGTCGCCGACGACCTGGGCTTCTCCGATATC GGCGCCTTCGGCGGCGAGATCGCCACGCCGAACCTCGACGCCCTGGCCATCGCCGGCCTG CGCCTGACCGACTTCCACACCGCCTCGACCTGCTCGCCGACCCGCTCGATGCTGCTCACC GGCACCGACCACCACATCGCCGGGATCGGCACCATGGCCGAGGCGCTGACCCCGGAACTG GAAGGCAAGCCGGGTTACGAAGGGCATCTCAACGAGCGCGTGGTGGCGCTGCCGGAGCTG CTCCGCGAGGCCGGCTACCAGACCCTCATGGCCGGCAAGTGGCACCTCGGTCTGAAGCCG GAACAGACGCCCCATGCACGCGGTTTCGAGCGTTCCTTCTCGCTGCTGCCGGGCGCCGCC AACCACTATGGTTTCGAGCCGCCCTACGACGAAAGCACTCCGCGCATCCTCAAGGGTACG CCAGCGCTCTACGTGGAAGACGAGCGCTACCTCGACACGCTGCCGGAGGGCTTCTATTCC TCCGACGCCTTCGGCGACAAGCTGCTGCAATACCTCAAGGAGCGCGACCAGAGCCGGCCG TTCTTCGCCTACCTGCCGTTCTCCGCGCCGCACTGGCCGCTGCAAGCGCCGCGGGAGATC GTCGAGAAGTACCGCGGTCGCTACGACGCCGGTCCAGAAGCGCTGCGCCAGGAACGCCTG GCCCGGCTCAAGGAGCTGGGCCTGGTGGAAGCGGACGTCGAAGCCCATCCGGTGCTCGCC CTGACCCGCGAGTGGGAGGCCCTGGAGGACGAGGAACGGGCTAAGTCGGCGCGGGCGATG GAGGTCTACGCGGCGATGGTCGAGCGCATGGACTGGAACATCGGCAGGGTCGTGGACTAC CTGCGCCGGCAGGGCGAGCTGGACAACACCTTCGTCCTGTTCATGTCCGACAACGGCGCC GAAGGCGCCCTGCTGGAGGCGTTCCCGAAATTCGGCCCGGACCTGCTGGGCTTTCTCGAC CGGCACTACGACAACAGCCTGGAAAACATCGGCCGCGCCAATTCCTACGTCTGGTATGGC CCGCGCTGGGCCCAGGCGGCCACCGCACCATCGCGCCTGTACAAGGCGTTCACCACCCAG GGCGGGATTCGCGTGCCAGCGCTGGTGCGCTACCCGCGGCTAAGCCGGCAGGGTGCGATC AGCCATGCCTTCGCCACGGTGATGGACGTCACCCCGACCCTCCTCGACCTCGCCGGTGTC CGCCACCCAGGCAAGCGCTGGCGCGGCCGCGAGATCGCCGAGCCGCGCGGCAGGTCGTGG CTGGGTTGGCTTTCCGGCGAGACCGAGGCGGCCCACGACGAGAACACCGTGACCGGCTGG GAGCTGTTCGGCATGCGTGCGATCCGCCAGGGCGACTGGAAGGCGGTGTACCTGCCGGCC CCGGTGGGCCCGGCCACCTGGCAGCTCTACGACCTGGCCCGCGACCCGGGCGAGATCCAC GACCTCGCTGACAGCCAGCCGGGCAAGCTGGCGGAGCTGATCGAGCATTGGAAGCGATAC GTCAGCGAGACCGGTGTCGTAGAGGGGGCTTCGCCTTTCCTGGTGCGATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P51691 UniProtKB Entry Name ARS_PSEAE GenBank Protein ID 5730324 GenBank Gene ID Z48540 - General References
- Beil S, Kehrli H, James P, Staudenmann W, Cook AM, Leisinger T, Kertesz MA: Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA). Eur J Biochem. 1995 Apr 15;229(2):385-94. [Article]
- Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
- Boltes I, Czapinska H, Kahnert A, von Bulow R, Dierks T, Schmidt B, von Figura K, Kertesz MA, Uson I: 1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. Structure. 2001 Jun;9(6):483-91. [Article]