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Oxidized polyvinyl alcohol hydrolase (OPH) (Oxidized PVA hydrolase) (EC 3.7.1.7) (Beta-diketone hydrolase)

 OPH_SPHS1               Reviewed;         364 AA.
Q588Z2;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
02-NOV-2016, entry version 26.
RecName: Full=Oxidized polyvinyl alcohol hydrolase;
Short=OPH;
Short=Oxidized PVA hydrolase;
EC=3.7.1.7;
AltName: Full=Beta-diketone hydrolase;
Flags: Precursor;
Name=oph;
Sphingopyxis sp. (strain 113P3).
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Sphingopyxis.
NCBI_TaxID=292913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-49 AND
222-230, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=113P3;
PubMed=15817792; DOI=10.1099/mic.0.27655-0;
Klomklang W., Tani A., Kimbara K., Mamoto R., Ueda T., Shimao M.,
Kawai F.;
"Biochemical and molecular characterization of a periplasmic hydrolase
for oxidized polyvinyl alcohol from Sphingomonas sp. strain 113P3.";
Microbiology 151:1255-1262(2005).
-!- FUNCTION: Catalyzes the hydrolysis of 4,6-nonanedione, a beta-
diketone compound. Also mediates hydrolysis of oxidized polyvinyl
alcohol (PVA) in the second step in the degradation of polyvinyl
alcohol. Not active toward the monoketone structure.
{ECO:0000269|PubMed:15817792}.
-!- CATALYTIC ACTIVITY: Nonane-4,6-dione + H(2)O = pentan-2-one +
butanoate. {ECO:0000269|PubMed:15817792}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.2 mM for polyvinyl alcohol {ECO:0000269|PubMed:15817792};
KM=0.3 mM for p-nitrophenyl acetate
{ECO:0000269|PubMed:15817792};
Vmax=0.1 umol/min/mg enzyme with polyvinyl alcohol as substrate
{ECO:0000269|PubMed:15817792};
Vmax=3.4 umol/min/mg enzyme with p-nitrophenyl acetate as
substrate {ECO:0000269|PubMed:15817792};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:15817792};
Temperature dependence:
Optimum temperature is 37 degrees Celsius.
{ECO:0000269|PubMed:15817792};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15817792}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15817792}.
-!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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EMBL; AB190288; BAD95542.3; -; Genomic_DNA.
PDB; 3WLA; X-ray; 1.90 A; A/B/C=35-364.
PDBsum; 3WLA; -.
ProteinModelPortal; Q588Z2; -.
SMR; Q588Z2; -.
ESTHER; sphs1-OPH; AlphaBeta_hydrolase.
BioCyc; MetaCyc:MONOMER-15499; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0047699; F:beta-diketone hydrolase activity; IEA:UniProtKB-EC.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Hydrolase; Periplasm; Signal.
SIGNAL 1 34 {ECO:0000269|PubMed:15817792}.
CHAIN 35 364 Oxidized polyvinyl alcohol hydrolase.
/FTId=PRO_0000419458.
ACT_SITE 190 190 Charge relay system. {ECO:0000250}.
ACT_SITE 293 293 Charge relay system. {ECO:0000250}.
STRAND 48 56 {ECO:0000244|PDB:3WLA}.
STRAND 59 66 {ECO:0000244|PDB:3WLA}.
STRAND 72 81 {ECO:0000244|PDB:3WLA}.
STRAND 84 86 {ECO:0000244|PDB:3WLA}.
HELIX 88 93 {ECO:0000244|PDB:3WLA}.
HELIX 95 97 {ECO:0000244|PDB:3WLA}.
HELIX 100 106 {ECO:0000244|PDB:3WLA}.
STRAND 109 113 {ECO:0000244|PDB:3WLA}.
HELIX 116 118 {ECO:0000244|PDB:3WLA}.
HELIX 127 129 {ECO:0000244|PDB:3WLA}.
STRAND 130 132 {ECO:0000244|PDB:3WLA}.
STRAND 137 142 {ECO:0000244|PDB:3WLA}.
HELIX 150 156 {ECO:0000244|PDB:3WLA}.
HELIX 161 173 {ECO:0000244|PDB:3WLA}.
TURN 174 176 {ECO:0000244|PDB:3WLA}.
STRAND 179 189 {ECO:0000244|PDB:3WLA}.
HELIX 191 202 {ECO:0000244|PDB:3WLA}.
TURN 204 206 {ECO:0000244|PDB:3WLA}.
STRAND 208 214 {ECO:0000244|PDB:3WLA}.
HELIX 229 238 {ECO:0000244|PDB:3WLA}.
STRAND 259 266 {ECO:0000244|PDB:3WLA}.
STRAND 272 274 {ECO:0000244|PDB:3WLA}.
TURN 277 279 {ECO:0000244|PDB:3WLA}.
STRAND 281 284 {ECO:0000244|PDB:3WLA}.
HELIX 285 297 {ECO:0000244|PDB:3WLA}.
STRAND 302 308 {ECO:0000244|PDB:3WLA}.
STRAND 313 315 {ECO:0000244|PDB:3WLA}.
HELIX 320 332 {ECO:0000244|PDB:3WLA}.
HELIX 340 342 {ECO:0000244|PDB:3WLA}.
STRAND 353 358 {ECO:0000244|PDB:3WLA}.
STRAND 360 362 {ECO:0000244|PDB:3WLA}.
SEQUENCE 364 AA; 39401 MW; 401909509D3F82F8 CRC64;
MFKPVVKSRS SRSFCYLAGC LAMVAATLSS TAQAKSEWAC PEGFTPKAGL NTDFPSDGKK
RAFVVVPPKD SAGGAPVWVP MVGTVEATNW NLNVPRSGNN AKLAEHGYMV ISPVRQCAEQ
DPNLGAGACN GVGKDGWTWN PWNDGRAPDA SGDKYKTDAG DDVRFLEAMV RCVGTKWKLD
RKRLFLGGIS AGGTMTNRAL LFDSEFWAGG MPISGEWYST KDDGSTVPFQ ETRKMVAAAP
AKIWQGRVGP YPLPSKLDPM VVITVWGGEK DLWDCGPPLG LCSDYRPTTQ ASSNYFSSIS
NVVHVACSAT HGHMWPQVNT DAFNLWALNT MASHPKGSSP KDFKLTAPPE GYSCKIGRFT
DHYK


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