OLHYD_STRPZ
ID OLHYD_STRPZ Reviewed; 590 AA.
AC B5XK69;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 58.
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;
DE AltName: Full=Linoleate hydratase;
DE AltName: Full=Myosin cross-reactive antigen;
DE Short=MCRA;
GN Name=sph; OrderedLocusNames=Spy49_0398;
OS Streptococcus pyogenes serotype M49 (strain NZ131).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=471876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ131;
RX PubMed=18820018; DOI=10.1128/jb.00672-08;
RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT Streptococcus pyogenes.";
RL J. Bacteriol. 190:7773-7785(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
RP PARAMETERS, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=591;
RX PubMed=20145247; DOI=10.1074/jbc.m109.081851;
RA Volkov A., Liavonchanka A., Kamneva O., Fiedler T., Goebel C.,
RA Kreikemeyer B., Feussner I.;
RT "Myosin cross-reactive antigen of Streptococcus pyogenes M49 encodes a
RT fatty acid double bond hydratase that plays a role in oleic acid
RT detoxification and bacterial virulence.";
RL J. Biol. Chem. 285:10353-10361(2010).
CC -!- FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to
CC yield 10-hydroxyoctadecanoate, and of linoleate at its cis-9- and cis-
CC 12-double bond to yield 10-hydroxy-12-octadecenoate and 10,13-
CC dihydroxyoctadecanoate. Is not active on trans-double bonds and
CC esterified fatty acids as substrate; is only active on cis-9- and/or
CC cis-12-double bond of C16 and C18 fatty acids without any trans-
CC configurations, producing 10-hydroxy and 10,13-dihydroxy derivatives.
CC Appears to play a role in oleic acid detoxification and bacterial
CC virulence. {ECO:0000269|PubMed:20145247}.
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:20145247};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20145247};
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:20145247};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for oleate {ECO:0000269|PubMed:20145247};
CC KM=49 uM for linoleate {ECO:0000269|PubMed:20145247};
CC Note=kcat is 67 min(-1) and 101 min(-1) with oleate and linoleate as
CC substrate, respectively.;
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Monomer and homodimer. Both forms seem to be active.
CC {ECO:0000269|PubMed:20145247}.
CC -!- DISRUPTION PHENOTYPE: In strain lacking this gene, consumption of the
CC free fatty acids from the medium is reduced to about 50% of that of the
CC wild-type. The mutant strain also appears to be 2-fold more sensitive
CC to oleic acid than wild-type, whereas no changes in sensitivity to
CC linoleic acid is observed. The mutant shows increased survival in blood
CC with reduced adherence and internalization to human keratinocytes.
CC {ECO:0000269|PubMed:20145247}.
CC -!- MISCELLANEOUS: Unsaturated fatty acids are toxic for many bacteria due
CC to deteriorating effect on bacterial cellular membrane and disruption
CC of bacterial fatty acid synthesis. The hydration of unsaturated fatty
CC acids is suggested to be a detoxification mechanism and a survival
CC strategy for living in fatty acid-rich environments (PubMed:20145247).
CC {ECO:0000305|PubMed:20145247}.
CC -!- SIMILARITY: Belongs to the oleate hydratase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACI60731.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000829; ACI60731.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044555196.1; NC_011375.1.
DR AlphaFoldDB; B5XK69; -.
DR SMR; B5XK69; -.
DR EnsemblBacteria; ACI60731; ACI60731; Spy49_0398.
DR KEGG; soz:Spy49_0398; -.
DR HOGENOM; CLU_024043_2_0_9; -.
DR BRENDA; 4.2.1.53; 5935.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001039; 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; -; 3.
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.
FT CHAIN 1..590
FT /note="Oleate hydratase"
FT /id="PRO_0000416455"
FT BINDING 29..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ 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
