OPH_SPHS1
ID OPH_SPHS1 Reviewed; 364 AA.
AC Q588Z2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Oxidized polyvinyl alcohol hydrolase;
DE Short=OPH;
DE Short=Oxidized PVA hydrolase;
DE EC=3.7.1.7;
DE AltName: Full=Beta-diketone hydrolase;
DE Flags: Precursor;
GN Name=oph;
OS Sphingopyxis sp. (strain 113P3).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=292913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-49 AND 222-230,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=113P3;
RX PubMed=15817792; DOI=10.1099/mic.0.27655-0;
RA Klomklang W., Tani A., Kimbara K., Mamoto R., Ueda T., Shimao M., Kawai F.;
RT "Biochemical and molecular characterization of a periplasmic hydrolase for
RT oxidized polyvinyl alcohol from Sphingomonas sp. strain 113P3.";
RL Microbiology 151:1255-1262(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of 4,6-nonanedione, a beta-diketone
CC compound. Also mediates hydrolysis of oxidized polyvinyl alcohol (PVA)
CC in the second step in the degradation of polyvinyl alcohol. Not active
CC toward the monoketone structure. {ECO:0000269|PubMed:15817792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + nonane-4,6-dione = butanoate + H(+) + pentan-2-one;
CC Xref=Rhea:RHEA:11908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16111, ChEBI:CHEBI:16472, ChEBI:CHEBI:17968; EC=3.7.1.7;
CC Evidence={ECO:0000269|PubMed:15817792};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for polyvinyl alcohol {ECO:0000269|PubMed:15817792};
CC KM=0.3 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:15817792};
CC Vmax=0.1 umol/min/mg enzyme with polyvinyl alcohol as substrate
CC {ECO:0000269|PubMed:15817792};
CC Vmax=3.4 umol/min/mg enzyme with p-nitrophenyl acetate as substrate
CC {ECO:0000269|PubMed:15817792};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15817792};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15817792};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15817792}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:15817792}.
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; AB190288; BAD95542.3; -; Genomic_DNA.
DR PDB; 3WLA; X-ray; 1.90 A; A/B/C=35-364.
DR PDBsum; 3WLA; -.
DR AlphaFoldDB; Q588Z2; -.
DR SMR; Q588Z2; -.
DR STRING; 292913.LH20_00825; -.
DR ESTHER; sphs1-OPH; AlphaBeta_hydrolase.
DR BioCyc; MetaCyc:MON-15499; -.
DR BRENDA; 3.7.1.7; 8996.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047699; F:beta-diketone hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Periplasm; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:15817792"
FT CHAIN 35..364
FT /note="Oxidized polyvinyl alcohol hydrolase"
FT /id="PRO_0000419458"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:3WLA"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:3WLA"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3WLA"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:3WLA"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:3WLA"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3WLA"
SQ 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
