ACYP_SACS2
ID ACYP_SACS2 Reviewed; 101 AA.
AC Q97ZL0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=SSO0887;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS), STRUCTURE BY NMR,
RP BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ACTIVE SITE.
RX PubMed=16287076; DOI=10.1002/prot.20703;
RA Corazza A., Rosano C., Pagano K., Alverdi V., Esposito G., Capanni C.,
RA Bemporad F., Plakoutsi G., Stefani M., Chiti F., Zuccotti S., Bolognesi M.,
RA Viglino P.;
RT "Structure, conformational stability, and enzymatic properties of
RT acylphosphatase from the hyperthermophile Sulfolobus solfataricus.";
RL Proteins 62:64-79(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for benzoylphosphate at 25 degrees Celsius
CC {ECO:0000269|PubMed:16287076};
CC pH dependence:
CC Optimum pH is 4.7-5.7. {ECO:0000269|PubMed:16287076};
CC Temperature dependence:
CC Optimum temperature is 81 degrees Celsius. Thermostable up to 100.8
CC degrees Celsius. Poorly active at 25 degrees Celsius. Enzymatic
CC activity is increased 4-fold by temperature increase from 25 to 45
CC degrees Celsius and more than 9-fold at 98 degrees Celsius.
CC {ECO:0000269|PubMed:16287076};
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; AE006641; AAK41170.1; -; Genomic_DNA.
DR PIR; C90239; C90239.
DR PDB; 1Y9O; NMR; -; A=1-101.
DR PDB; 2BJD; X-ray; 1.27 A; A/B=1-101.
DR PDB; 2BJE; X-ray; 1.90 A; A/C/E/G=1-101.
DR PDB; 4OIX; X-ray; 1.55 A; A=1-101.
DR PDB; 4OJ1; X-ray; 1.70 A; A/B=1-101.
DR PDB; 4OJ3; X-ray; 2.20 A; A/B=1-101.
DR PDB; 4OJG; X-ray; 1.38 A; A/B=1-101.
DR PDB; 4OJH; X-ray; 1.60 A; A/B=1-101.
DR PDBsum; 1Y9O; -.
DR PDBsum; 2BJD; -.
DR PDBsum; 2BJE; -.
DR PDBsum; 4OIX; -.
DR PDBsum; 4OJ1; -.
DR PDBsum; 4OJ3; -.
DR PDBsum; 4OJG; -.
DR PDBsum; 4OJH; -.
DR AlphaFoldDB; Q97ZL0; -.
DR BMRB; Q97ZL0; -.
DR SMR; Q97ZL0; -.
DR MINT; Q97ZL0; -.
DR STRING; 273057.SSO0887; -.
DR PRIDE; Q97ZL0; -.
DR EnsemblBacteria; AAK41170; AAK41170; SSO0887.
DR KEGG; sso:SSO0887; -.
DR PATRIC; fig|273057.12.peg.891; -.
DR eggNOG; arCOG01674; Archaea.
DR HOGENOM; CLU_141932_2_1_2; -.
DR InParanoid; Q97ZL0; -.
DR OMA; VGFRWSM; -.
DR PhylomeDB; Q97ZL0; -.
DR BRENDA; 3.6.1.7; 6163.
DR SABIO-RK; Q97ZL0; -.
DR EvolutionaryTrace; Q97ZL0; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR DisProt; DP00513; -.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR47268; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..101
FT /note="Acylphosphatase"
FT /id="PRO_0000326870"
FT DOMAIN 15..101
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 30
FT /evidence="ECO:0000269|PubMed:16287076"
FT ACT_SITE 48
FT /evidence="ECO:0000269|PubMed:16287076"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:4OJ3"
FT STRAND 13..23
FT /evidence="ECO:0007829|PDB:2BJD"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2BJD"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:2BJD"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2BJD"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1Y9O"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:2BJD"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2BJD"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:2BJD"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2BJD"
SQ SEQUENCE 101 AA; 11636 MW; 9BC4BF537EA7B4FA CRC64;
MKKWSDTEVF EMLKRMYARV YGLVQGVGFR KFVQIHAIRL GIKGYAKNLP DGSVEVVAEG
YEEALSKLLE RIKQGPPAAE VEKVDYSFSE YKGEFEDFET Y
