OLHYD_MACCJ
ID OLHYD_MACCJ Reviewed; 589 AA.
AC B9E972;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Oleate hydratase;
DE EC=4.2.1.53;
DE AltName: Full=Fatty acid double bond hydratase;
DE AltName: Full=Fatty acid hydratase;
GN OrderedLocusNames=MCCL_0076;
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402;
RX PubMed=19074389; DOI=10.1128/jb.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLY-29; GLY-31;
RP SER-34; GLU-50 AND GLU-56.
RC STRAIN=KCTC 3582;
RX PubMed=22203098; DOI=10.1016/j.biochi.2011.12.011;
RA Joo Y.C., Jeong K.W., Yeom S.J., Kim Y.S., Kim Y., Oh D.K.;
RT "Biochemical characterization and FAD-binding analysis of oleate hydratase
RT from Macrococcus caseolyticus.";
RL Biochimie 94:907-915(2012).
CC -!- FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to
CC yield 10-hydroxyoctadecanoate. Cannot catalyze the reverse reaction. Is
CC not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-
CC 8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty
CC acids as substrate; is only active on cis-9- and/or cis-12-double bond
CC of unsaturated fatty acids without any trans-configurations, producing
CC 10-hydroxy and 10,13-dihydroxy fatty acids. The hydration of
CC unsaturated fatty acids is suggested to be a detoxification mechanism
CC and a survival strategy for living in fatty acid-rich environments.
CC {ECO:0000269|PubMed:22203098}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O;
CC Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683,
CC ChEBI:CHEBI:30823; EC=4.2.1.53;
CC Evidence={ECO:0000269|PubMed:22203098};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:22203098};
CC Note=Binds 1 FAD per subunit. FAD does not seem to be involved in
CC catalysis but rather in the structural stabilization of the enzyme.
CC {ECO:0000269|PubMed:22203098};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=340 uM for oleate {ECO:0000269|PubMed:22203098};
CC KM=300 uM for myristoleate {ECO:0000269|PubMed:22203098};
CC KM=570 uM for palmitoleate {ECO:0000269|PubMed:22203098};
CC KM=390 uM for linoleate {ECO:0000269|PubMed:22203098};
CC KM=320 uM for alpha-linolenate {ECO:0000269|PubMed:22203098};
CC KM=590 uM for gamma-linolenate {ECO:0000269|PubMed:22203098};
CC Note=kcat is 470 min(-1) with oleate as substrate. The catalytic
CC efficiency with oleate as substrate is 3.5-fold higher than that with
CC palmitoleate, the second favored substrate.;
CC pH dependence:
CC Optimum pH is 6.5 with oleate as substrate.
CC {ECO:0000269|PubMed:22203098};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius with oleate as substrate.
CC After 120 minutes, the enzyme activity is nearly unchanged at 25
CC degrees Celsius, but is reduced to only 25% at 35 degrees Celsius.
CC {ECO:0000269|PubMed:22203098};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22203098}.
CC -!- SIMILARITY: Belongs to the oleate hydratase family. {ECO:0000305}.
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DR EMBL; AP009484; BAH16783.1; -; Genomic_DNA.
DR RefSeq; WP_012655987.1; NC_011999.1.
DR AlphaFoldDB; B9E972; -.
DR SMR; B9E972; -.
DR STRING; 458233.MCCL_0076; -.
DR PRIDE; B9E972; -.
DR EnsemblBacteria; BAH16783; BAH16783; MCCL_0076.
DR KEGG; mcl:MCCL_0076; -.
DR eggNOG; COG4716; Bacteria.
DR HOGENOM; CLU_024043_2_0_9; -.
DR OMA; CRLIHKR; -.
DR OrthoDB; 123225at2; -.
DR BRENDA; 4.2.1.53; 3338.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001383; Chromosome.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0050151; F:oleate hydratase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010354; Oleate_hydratase.
DR PANTHER; PTHR37417; PTHR37417; 1.
DR Pfam; PF06100; MCRA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Detoxification; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Lyase; Reference proteome.
FT CHAIN 1..589
FT /note="Oleate hydratase"
FT /id="PRO_0000416453"
FT BINDING 29..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT MUTAGEN 29
FT /note="G->A: Large decrease in FAD-binding and loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22203098"
FT MUTAGEN 31
FT /note="G->A: Large decrease in FAD-binding and loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22203098"
FT MUTAGEN 34
FT /note="S->A: 1.7-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22203098"
FT MUTAGEN 50
FT /note="E->A: Nearly no effect on catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22203098"
FT MUTAGEN 56
FT /note="E->A: Large decrease in FAD-binding and loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22203098"
SQ SEQUENCE 589 AA; 67309 MW; EB20282C90DA2072 CRC64;
MYYSNGNYEA FARPKKPEGV DNKSAYLVGS GLASLAAASF LIRDGQMKGE NIHILEELDL
PGGSLDGILN PERGYIMRGG REMENHFECL WDLFRSVPSL EVEDASVLDE FYWLNKEDPN
YSKCRVIENR GQRLESDGKM TLTKKANKEI IQLCLMKEEQ LNDVKISDVF SKDFLDSNFW
IYWKTMFAFE PWHSAMEMRR YLMRFIHHIG GLADFSALKF TKFNQFESLV MPLIEHLKAK
NVTFEYGVTV KNIQVECSKE SKVAKAIDIV RRGNEESIPL TENDLVFVTN GSITESTTYG
DNDTPAPPTS KPGGAWQLWE NLSTQCEEFG NPAKFYKDLP EKSWFVSATA TTNNKEVIDY
IQKICKRDPL SGRTVTGGIV TVDDSNWQLS FTLNRQQQFK NQPDDQVSVW IYALYSDERG
ERTNKTIVEC SGKEICEEWL YHMGVPEEKI SALAAECNTI PSYMPYITAY FMPRKEGDRP
LVVPHGSKNI AFIGNFAETE RDTVFTTEYS VRTAMEAVYK LLEVDRGVPE VFASVYDVRI
LLHALSVLND GKKLDEIDMP FYERLVEKRL LKKASGTFIE ELLEEANLI
