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Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (Linoleate hydratase) (Myosin cross-reactive antigen) (MCRA)

 OLHYD_STRPZ             Reviewed;         590 AA.
B5XK69;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 2.
22-NOV-2017, entry version 44.
RecName: Full=Oleate hydratase;
EC=4.2.1.53;
AltName: Full=Fatty acid double bond hydratase;
AltName: Full=Fatty acid hydratase;
AltName: Full=Linoleate hydratase;
AltName: Full=Myosin cross-reactive antigen;
Short=MCRA;
Name=sph; OrderedLocusNames=Spy49_0398;
Streptococcus pyogenes serotype M49 (strain NZ131).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=471876;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NZ131;
PubMed=18820018; DOI=10.1128/JB.00672-08;
McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
"Genome sequence of a nephritogenic and highly transformable M49
strain of Streptococcus pyogenes.";
J. Bacteriol. 190:7773-7785(2008).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
PARAMETERS, DISRUPTION PHENOTYPE, AND SUBUNIT.
STRAIN=591;
PubMed=20145247; DOI=10.1074/jbc.M109.081851;
Volkov A., Liavonchanka A., Kamneva O., Fiedler T., Goebel C.,
Kreikemeyer B., Feussner I.;
"Myosin cross-reactive antigen of Streptococcus pyogenes M49 encodes a
fatty acid double bond hydratase that plays a role in oleic acid
detoxification and bacterial virulence.";
J. Biol. Chem. 285:10353-10361(2010).
-!- FUNCTION: Catalyzes the hydration of oleate at its cis-9-double
bond to yield 10-hydroxyoctadecanoate, and of linoleate at its
cis-9- and cis-12-double bond to yield 10-hydroxy-12-octadecenoate
and 10,13-dihydroxyoctadecanoate. Is not active on trans-double
bonds and esterified fatty acids as substrate; is only active on
cis-9- and/or cis-12-double bond of C16 and C18 fatty acids
without any trans-configurations, producing 10-hydroxy and 10,13-
dihydroxy derivatives. Appears to play a role in oleic acid
detoxification and bacterial virulence.
{ECO:0000269|PubMed:20145247}.
-!- CATALYTIC ACTIVITY: (R)-10-hydroxystearate = oleate + H(2)O.
{ECO:0000269|PubMed:20145247}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:20145247};
Note=Binds 1 FAD per subunit. FAD does not seem to be involved in
catalysis but rather in the structural stabilization of the
enzyme. {ECO:0000269|PubMed:20145247};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=63 uM for oleate {ECO:0000269|PubMed:20145247};
KM=49 uM for linoleate {ECO:0000269|PubMed:20145247};
Note=kcat is 67 min(-1) and 101 min(-1) with oleate and
linoleate as substrate, respectively.;
-!- PATHWAY: Lipid metabolism; fatty acid metabolism.
-!- SUBUNIT: Monomer and homodimer. Both forms seem to be active.
{ECO:0000269|PubMed:20145247}.
-!- DISRUPTION PHENOTYPE: In strain lacking this gene, consumption of
the free fatty acids from the medium is reduced to about 50% of
that of the wild-type. The mutant strain also appears to be 2-fold
more sensitive to oleic acid than wild-type, whereas no changes in
sensitivity to linoleic acid is observed. The mutant shows
increased survival in blood with reduced adherence and
internalization to human keratinocytes.
{ECO:0000269|PubMed:20145247}.
-!- MISCELLANEOUS: Unsaturated fatty acids are toxic for many bacteria
due to deteriorating effect on bacterial cellular membrane and
disruption of bacterial fatty acid synthesis. The hydration of
unsaturated fatty acids is suggested to be a detoxification
mechanism and a survival strategy for living in fatty acid-rich
environments (PubMed:20145247). {ECO:0000305|PubMed:20145247}.
-!- SIMILARITY: Belongs to the oleate hydratase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ACI60731.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; CP000829; ACI60731.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_044555196.1; NC_011375.1.
SMR; B5XK69; -.
EnsemblBacteria; ACI60731; ACI60731; Spy49_0398.
KEGG; soz:Spy49_0398; -.
HOGENOM; HOG000237402; -.
KO; K10254; -.
UniPathway; UPA00199; -.
Proteomes; UP000001039; Chromosome.
GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0050151; F:oleate hydratase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR010354; Oleate_hydratase.
PANTHER; PTHR37417; PTHR37417; 1.
Pfam; PF06100; MCRA; 1.
SUPFAM; SSF51905; SSF51905; 1.
1: Evidence at protein level;
Complete proteome; Detoxification; FAD; Fatty acid metabolism;
Flavoprotein; Lipid metabolism; Lyase.
CHAIN 1 590 Oleate hydratase.
/FTId=PRO_0000416455.
NP_BIND 29 34 FAD. {ECO:0000250}.
BINDING 56 56 FAD. {ECO:0000250}.
SEQUENCE 590 AA; 67408 MW; AC10179333C69C96 CRC64;
MYYTSGNYEA FATPRKPEGV DQKSAYIVGT GLAGLAAAVF LIRDGHMAGE RIHLFEELPL
AGGSLDGIEK PHLGFVTRGG REMENHFECM WDMYRSIPSL EIPGASYLDE FYWLDKDDPN
SSNCRLIHKR GNRVDDDGQY TLGKQSKELI HLIMKTEESL GDQTIEEFFS EDFFKSNFWV
YWATMFAFEK WHSAVEMRRY AMRFIHHIDG LPDFTSLKFN KYNQYDSMVK PIIAYLESHD
VDIQFDTKVT DIQVEQTAGK KVAKTIHMTV SGEAKAIELT PDDLVFVTNG SITESSTYGS
HHEVAKPTKA LGGSWNLWEN LAAQSDDFGH PKVFYQDLPA ESWFVSATAT IKHPAIEPYI
ERLTHRDLHD GKVNTGGIIT ITDSNWMMSF AIHRQPHFKE QKENETTVWI YGLYSNSEGN
YVHKKIEECT GQEITEEWLY HLGVPVDKIK DLASQEYINT VPVYMPYITS YFMPRVKGDR
PKVIPDGSVN LAFIGNFAES PSRDTVFTTE YSIRTAMEAV YSFLNGERGI PQGFNSAYDI
RELLKAFYYL NDKKAIKDMD LPIPALIEKI GHKKIKDTFI EELLKDANLM


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