ACYP_PYRHO
ID ACYP_PYRHO Reviewed; 91 AA.
AC P84142;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=PH0305.1;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=15213401; DOI=10.1107/s0907444904010996;
RA Cheung Y.-Y., Allen M.D., Bycroft M., Wong K.-B.;
RT "Crystallization and preliminary crystallographic analysis of an
RT acylphosphatase from the hyperthermophilic archaeon Pyrococcus
RT horikoshii.";
RL Acta Crystallogr. D 60:1308-1310(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
RX PubMed=15159579; DOI=10.1107/s0907444904007735;
RA Miyazono K.I., Kudo N., Tanokura M.;
RT "Cloning, purification, crystallization and preliminary crystallographic
RT analysis of acylphosphatase from Pyrococcus horikoshii OT3.";
RL Acta Crystallogr. D 60:1135-1136(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=15779887; DOI=10.1021/bi047832k;
RA Cheung Y.-Y., Lam S.Y., Chu W.-K., Allen M.D., Bycroft M., Wong K.-B.;
RT "Crystal structure of a hyperthermophilic archaeal acylphosphatase from
RT Pyrococcus horikoshii -- structural insights into enzymatic catalysis,
RT thermostability, and dimerization.";
RL Biochemistry 44:4601-4611(2005).
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=0.12 mM for benzoylphosphate at 25 degrees Celsius
CC {ECO:0000269|PubMed:15779887};
CC pH dependence:
CC Optimum pH is 5.3 at 25 degrees Celsius.
CC {ECO:0000269|PubMed:15779887};
CC Temperature dependence:
CC Optimum temperature is 98 degrees Celsius. Poorly active at 25
CC degrees Celsius. Thermostable up to 100 degrees Celsius.
CC {ECO:0000269|PubMed:15779887};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15779887}.
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; BA000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_010884399.1; NC_000961.1.
DR PDB; 1V3Z; X-ray; 1.72 A; A/B=1-91.
DR PDB; 1W2I; X-ray; 1.50 A; A/B=1-91.
DR PDB; 2W4D; X-ray; 2.40 A; A/B/C/D/E/F=2-91.
DR PDB; 3TNV; X-ray; 1.60 A; A=1-91.
DR PDBsum; 1V3Z; -.
DR PDBsum; 1W2I; -.
DR PDBsum; 2W4D; -.
DR PDBsum; 3TNV; -.
DR AlphaFoldDB; P84142; -.
DR SMR; P84142; -.
DR GeneID; 1444186; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 111329at2157; -.
DR BRENDA; 3.6.1.7; 5244.
DR SABIO-RK; P84142; -.
DR EvolutionaryTrace; P84142; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB.
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 PRINTS; PR00112; ACYLPHPHTASE.
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.
FT CHAIN 1..91
FT /note="Acylphosphatase"
FT /id="PRO_0000158560"
FT DOMAIN 5..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 20
FT /evidence="ECO:0000269|PubMed:15779887"
FT ACT_SITE 38
FT /evidence="ECO:0000269|PubMed:15779887"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1W2I"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1W2I"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1W2I"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1W2I"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1W2I"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1W2I"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1W2I"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:1W2I"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1W2I"
SQ SEQUENCE 91 AA; 10260 MW; 6DDB6B69DBA17087 CRC64;
MAIVRAHLKI YGRVQGVGFR WSMQREARKL GVNGWVRNLP DGSVEAVLEG DEERVEALIG
WAHQGPPLAR VTRVEVKWEQ PKGEKGFRIV G
