FAH12_CLAPU
ID FAH12_CLAPU Reviewed; 477 AA.
AC B4YQU1; A0A1L7NQ89;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Oleate hydroxylase FAH12 {ECO:0000303|PubMed:18467452};
DE Short=CpFAH {ECO:0000303|PubMed:18467452};
DE Short=CpFAH12 {ECO:0000303|PubMed:22370951};
DE EC=1.14.-.- {ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951, ECO:0000269|PubMed:27830762};
DE AltName: Full=Oleate Delta(12)-hydroxylase {ECO:0000303|PubMed:18467452};
GN Name=FAH12 {ECO:0000303|PubMed:22370951};
GN Synonyms=FAH {ECO:0000303|PubMed:18467452};
OS Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=5111;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP BIOTECHNOLOGY.
RX PubMed=18467452; DOI=10.1104/pp.108.117168;
RA Meesapyodsuk D., Qiu X.;
RT "An oleate hydroxylase from the fungus Claviceps purpurea: cloning,
RT functional analysis, and expression in Arabidopsis.";
RL Plant Physiol. 147:1325-1333(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY,
RP AND PATHWAY.
RC STRAIN=NBRC 6263;
RX PubMed=27830762; DOI=10.1038/srep36809;
RA Kajikawa M., Abe T., Ifuku K., Furutani K., Yan D., Okuda T., Ando A.,
RA Kishino S., Ogawa J., Fukuzawa H.;
RT "Production of ricinoleic acid-containing monoestolide triacylglycerides in
RT an oleaginous diatom, Chaetoceros gracilis.";
RL Sci. Rep. 6:36809-36809(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, AND PATHWAY.
RX PubMed=22370951; DOI=10.1007/s00253-012-3959-6;
RA Holic R., Yazawa H., Kumagai H., Uemura H.;
RT "Engineered high content of ricinoleic acid in fission yeast
RT Schizosaccharomyces pombe.";
RL Appl. Microbiol. Biotechnol. 95:179-187(2012).
CC -!- FUNCTION: Oleate hydroxylase involved in the biosynthesis of
CC ricinoleate (PubMed:27830762, PubMed:22370951). Exhibits delta(12)
CC hydroxylase activity on 16C and 18C monounsaturated fatty acids (e.g.
CC oleic and palmitoleic acids), and, to a lower extent, gamma(3)
CC hydroxylase activity on ricinoleic acid (PubMed:18467452,
CC PubMed:27830762). It uses cytochrome b5 as an electron donor. May act
CC on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (By
CC similarity). {ECO:0000250|UniProtKB:Q41131,
CC ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951,
CC ECO:0000269|PubMed:27830762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + AH2 + O2 = (12R)-hydroxy-(9Z)-
CC octadecenoate + A + H2O; Xref=Rhea:RHEA:55956, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:91295;
CC Evidence={ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951,
CC ECO:0000269|PubMed:27830762};
CC -!- PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:18467452, ECO:0000269|PubMed:22370951,
CC ECO:0000269|PubMed:27830762}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q41131}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250|UniProtKB:D2CPE1}.
CC -!- BIOTECHNOLOGY: Mediates gamma(3) desaturated fatty acids (e.g.
CC densipolic acid) and ricinoleic acid accumulation when expressed in
CC S.pombe with a temperature-dependent toxicity, at 30 degrees Celsius
CC but not at 37 degrees Celsius. {ECO:0000269|PubMed:18467452,
CC ECO:0000269|PubMed:22370951, ECO:0000269|PubMed:27830762}.
CC -!- BIOTECHNOLOGY: Triggers hydroxyl fatty acids accumulation in seeds when
CC expressed in A.thaliana under the guidance of a seed-specific promoter.
CC {ECO:0000269|PubMed:18467452}.
CC -!- BIOTECHNOLOGY: Promotes ricinoleic acid biosynthesis when expressed in
CC C.gracilis. {ECO:0000269|PubMed:27830762}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EU661785; ACF37070.1; -; mRNA.
DR EMBL; LC149858; BAW27658.1; -; mRNA.
DR AlphaFoldDB; B4YQU1; -.
DR SwissLipids; SLP:000001882; -.
DR VEuPathDB; FungiDB:CPUR_04032; -.
DR BRENDA; 1.14.18.4; 1445.
DR UniPathway; UPA01038; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0102517; F:oleate 12-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0042389; F:omega-3 fatty acid desaturase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IDA:UniProtKB.
DR GO; GO:0050183; F:phosphatidylcholine 12-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..477
FT /note="Oleate hydroxylase FAH12"
FT /id="PRO_0000443444"
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..159
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:D2CPE1"
FT MOTIF 191..195
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:D2CPE1"
FT CONFLICT 327
FT /note="A -> T (in Ref. 2; BAW27658)"
SQ SEQUENCE 477 AA; 53452 MW; 4225600A194C2A13 CRC64;
MASATPAMSE NAVLRHKAAS TTGIDYESSA AVSPAESPRT SASSTSLSSL SSLDANEKKD
EYAGLLDTYG NAFTPPDFSI KDIRAAIPKH CYERSTIKSY AYVLRDLLCL STTFYLFHNF
VTPENIPSNP LRFVLWSIYT VLQGLFATGL WVIGHECGHC AFSPSPFISD LTGWVIHSAL
LVPYFSWKFS HSAHHKGIGN MERDMVFLPR TREQQATRLG RAVEELGDLC EETPIYTALH
LVGKQLIGWP SYLMTNATGH NFHERQREGR GKGKKNGFGG GVNHFDPRSP IFEARQAKYI
VLSDIGLGLA IAALVYLGNR FGWANMAVWY FLPYLWVNHW LVAITFLQHT DPTLPHYNRE
EWNFVRGGAC TIDRDLGFIG RHLFHGIADT HVVHHYVSRI PFYNADEASE AIKPIMGKHY
RSDTAHGPVG FLHALWKTAR WCQWVEPSAD AQGAGKGILF YRNRNKLGTK PISMKTQ
