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Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase)

 OLHYD_ELIME             Reviewed;         646 AA.
C7DLJ6;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 1.
28-FEB-2018, entry version 26.
RecName: Full=Oleate hydratase;
EC=4.2.1.53;
AltName: Full=Fatty acid double bond hydratase;
AltName: Full=Fatty acid hydratase;
Name=ohyA;
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Elizabethkingia.
NCBI_TaxID=238;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
SUBUNIT.
STRAIN=3266;
PubMed=19465645; DOI=10.1128/JB.00306-09;
Bevers L.E., Pinkse M.W., Verhaert P.D., Hagen W.R.;
"Oleate hydratase catalyzes the hydration of a nonactivated carbon-
carbon bond.";
J. Bacteriol. 191:5010-5012(2009).
-!- FUNCTION: Catalyzes the hydration of oleate at its cis-9-double
bond to yield 10-hydroxyoctadecanoate. The hydration of
unsaturated fatty acids is suggested to be a detoxification
mechanism and a survival strategy for living in fatty acid-rich
environments. {ECO:0000269|PubMed:19465645}.
-!- CATALYTIC ACTIVITY: (R)-10-hydroxystearate = oleate + H(2)O.
{ECO:0000269|PubMed:19465645}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
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:0000250};
-!- ENZYME REGULATION: Is not inhibited by EDTA in vitro.
{ECO:0000269|PubMed:19465645}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.21 mM for oleate (at 30 degrees Celsius)
{ECO:0000269|PubMed:19465645};
Vmax=0.170 umol/min/mg enzyme (at 30 degrees Celsius)
{ECO:0000269|PubMed:19465645};
Note=Due to the low solubility of oleate in Tris buffer, the
values given above are approximate, the real Vmax is most likely
significantly higher, whereas the real KM is expected to be much
lower.;
pH dependence:
Optimum pH is around 6. {ECO:0000269|PubMed:19465645};
-!- PATHWAY: Lipid metabolism; fatty acid metabolism.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19465645}.
-!- INDUCTION: Strongly up-regulated in cells grown in the presence of
oleate. {ECO:0000269|PubMed:19465645}.
-!- SIMILARITY: Belongs to the oleate hydratase family. {ECO:0000305}.
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EMBL; GQ144652; ACT54545.1; -; Genomic_DNA.
PDB; 4UIR; X-ray; 2.75 A; A/B=1-646.
PDBsum; 4UIR; -.
ProteinModelPortal; C7DLJ6; -.
SMR; C7DLJ6; -.
BRENDA; 4.2.1.53; 1374.
SABIO-RK; C7DLJ6; -.
UniPathway; UPA00199; -.
GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0050151; F:oleate hydratase activity; IDA:UniProtKB.
GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
Gene3D; 3.50.50.60; -; 2.
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;
3D-structure; Detoxification; FAD; Fatty acid metabolism;
Flavoprotein; Lipid metabolism; Lyase.
CHAIN 1 646 Oleate hydratase.
/FTId=PRO_0000416454.
NP_BIND 69 74 FAD. {ECO:0000250}.
BINDING 96 96 FAD. {ECO:0000250}.
TURN 3 5 {ECO:0000244|PDB:4UIR}.
HELIX 6 8 {ECO:0000244|PDB:4UIR}.
HELIX 9 12 {ECO:0000244|PDB:4UIR}.
TURN 27 29 {ECO:0000244|PDB:4UIR}.
HELIX 48 50 {ECO:0000244|PDB:4UIR}.
STRAND 65 68 {ECO:0000244|PDB:4UIR}.
HELIX 72 85 {ECO:0000244|PDB:4UIR}.
HELIX 89 91 {ECO:0000244|PDB:4UIR}.
STRAND 92 95 {ECO:0000244|PDB:4UIR}.
STRAND 97 100 {ECO:0000244|PDB:4UIR}.
TURN 101 104 {ECO:0000244|PDB:4UIR}.
STRAND 108 110 {ECO:0000244|PDB:4UIR}.
TURN 111 113 {ECO:0000244|PDB:4UIR}.
STRAND 114 116 {ECO:0000244|PDB:4UIR}.
HELIX 128 134 {ECO:0000244|PDB:4UIR}.
STRAND 140 142 {ECO:0000244|PDB:4UIR}.
HELIX 148 156 {ECO:0000244|PDB:4UIR}.
STRAND 157 159 {ECO:0000244|PDB:4UIR}.
STRAND 166 169 {ECO:0000244|PDB:4UIR}.
TURN 170 172 {ECO:0000244|PDB:4UIR}.
HELIX 184 195 {ECO:0000244|PDB:4UIR}.
HELIX 198 200 {ECO:0000244|PDB:4UIR}.
TURN 207 209 {ECO:0000244|PDB:4UIR}.
HELIX 212 216 {ECO:0000244|PDB:4UIR}.
HELIX 218 226 {ECO:0000244|PDB:4UIR}.
HELIX 235 244 {ECO:0000244|PDB:4UIR}.
HELIX 246 251 {ECO:0000244|PDB:4UIR}.
STRAND 252 254 {ECO:0000244|PDB:4UIR}.
HELIX 265 268 {ECO:0000244|PDB:4UIR}.
HELIX 270 280 {ECO:0000244|PDB:4UIR}.
STRAND 283 285 {ECO:0000244|PDB:4UIR}.
STRAND 288 297 {ECO:0000244|PDB:4UIR}.
STRAND 302 311 {ECO:0000244|PDB:4UIR}.
STRAND 316 319 {ECO:0000244|PDB:4UIR}.
STRAND 325 329 {ECO:0000244|PDB:4UIR}.
TURN 333 336 {ECO:0000244|PDB:4UIR}.
STRAND 338 341 {ECO:0000244|PDB:4UIR}.
TURN 353 356 {ECO:0000244|PDB:4UIR}.
HELIX 361 368 {ECO:0000244|PDB:4UIR}.
HELIX 372 374 {ECO:0000244|PDB:4UIR}.
HELIX 377 379 {ECO:0000244|PDB:4UIR}.
HELIX 384 387 {ECO:0000244|PDB:4UIR}.
STRAND 389 396 {ECO:0000244|PDB:4UIR}.
HELIX 400 408 {ECO:0000244|PDB:4UIR}.
STRAND 415 417 {ECO:0000244|PDB:4UIR}.
STRAND 424 426 {ECO:0000244|PDB:4UIR}.
STRAND 433 436 {ECO:0000244|PDB:4UIR}.
STRAND 451 458 {ECO:0000244|PDB:4UIR}.
STRAND 460 462 {ECO:0000244|PDB:4UIR}.
STRAND 465 467 {ECO:0000244|PDB:4UIR}.
HELIX 471 473 {ECO:0000244|PDB:4UIR}.
HELIX 476 487 {ECO:0000244|PDB:4UIR}.
HELIX 490 492 {ECO:0000244|PDB:4UIR}.
HELIX 493 498 {ECO:0000244|PDB:4UIR}.
STRAND 500 507 {ECO:0000244|PDB:4UIR}.
TURN 508 511 {ECO:0000244|PDB:4UIR}.
HELIX 512 514 {ECO:0000244|PDB:4UIR}.
STRAND 524 526 {ECO:0000244|PDB:4UIR}.
STRAND 530 537 {ECO:0000244|PDB:4UIR}.
STRAND 547 549 {ECO:0000244|PDB:4UIR}.
HELIX 550 564 {ECO:0000244|PDB:4UIR}.
HELIX 577 579 {ECO:0000244|PDB:4UIR}.
HELIX 581 591 {ECO:0000244|PDB:4UIR}.
TURN 592 594 {ECO:0000244|PDB:4UIR}.
HELIX 600 607 {ECO:0000244|PDB:4UIR}.
HELIX 613 615 {ECO:0000244|PDB:4UIR}.
HELIX 630 645 {ECO:0000244|PDB:4UIR}.
SEQUENCE 646 AA; 73488 MW; 2E48182DD936251D CRC64;
MNPITSKFDK VLNASSEYGH VNHEPDSSKE QQRNTPQKSM PFSDQIGNYQ RNKGIPVQSY
DNSKIYIIGS GIAGMSAAYY FIRDGHVPAK NITFLEQLHI DGGSLDGAGN PTDGYIIRGG
REMDMTYENL WDMFQDIPAL EMPAPYSVLD EYRLINDNDS NYSKARLINN KGEIKDFSKF
GLNKMDQLAI IRLLLKNKEE LDDLTIEDYF SESFLKSNFW TFWRTMFAFE NWHSLLELKL
YMHRFLHAID GLNDLSSLVF PKYNQYDTFV TPLRKFLQEK GVNIHLNTLV KDLDIHINTE
GKVVEGIITE QDGKEVKIPV GKNDYVIVTT GSMTEDTFYG NNKTAPIIGI DNSTSGQSAG
WKLWKNLAAK SEIFGKPEKF CSNIEKSAWE SATLTCKPSA LIDKLKEYSV NDPYSGKTVT
GGIITITDSN WLMSFTCNRQ PHFPEQPDDV LVLWVYALFM DKEGNYIKKT MLECTGDEIL
AELCYHLGIE DQLENVQKNT IVRTAFMPYI TSMFMPRAKG DRPRVVPEGC KNLGLVGQFV
ETNNDVVFTM ESSVRTARIA VYKLLNLNKQ VPDINPLQYD IRHLLKAAKT LNDDKPFVGE
GLLRKVLKGT YFEHVLPAGA AEEEEHESFI AEHVNKFREW VKGIRG


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