PFI_PTIFI
ID PFI_PTIFI Reviewed; 500 AA.
AC Q8W257; Q8W256;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Polyenoic fatty acid isomerase;
DE Short=PFI;
DE EC=5.3.3.13;
DE Flags: Precursor;
OS Ptilota filicina (Red alga).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Ceramiaceae; Ptilota.
OX NCBI_TaxID=153248;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zheng W., Wise M.L., Wyrick A., Metz J.G., Yuan L., Gerwick W.H.;
RT "Polyenoic fatty acid isomerase from the marine alga Ptilota filicina.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-59, FUNCTION, SUBUNIT,
RP GLYCOSYLATION, AND COFACTOR.
RX PubMed=12054482; DOI=10.1016/s0003-9861(02)00002-4;
RA Zheng W., Wise M.L., Wyrick A., Metz J.G., Yuan L., Gerwick W.H.;
RT "Polyenoic fatty acid isomerase from the marine alga Ptilota filicina:
RT protein characterization and functional expression of the cloned cDNA.";
RL Arch. Biochem. Biophys. 401:11-20(2002).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=7803384; DOI=10.1021/bi00255a002;
RA Wise M.L., Hamberg M., Gerwick W.H.;
RT "Biosynthesis of conjugated triene-containing fatty acids by a novel
RT isomerase from the red marine alga Ptilota filicina.";
RL Biochemistry 33:15223-15232(1994).
RN [4]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9062129; DOI=10.1021/bi962158v;
RA Wise M.L., Rossi J., Gerwick W.H.;
RT "Characterization of the substrate binding site of polyenoic fatty acid
RT isomerase, a novel enzyme from the marine alga Ptilota filicina.";
RL Biochemistry 36:2985-2992(1997).
CC -!- FUNCTION: Involved in the biosynthesis of conjugated triene-containing
CC fatty acids. Catalyzes the isomerization of a wide range of substrates
CC containing three or more methylene interrupted olefins into a Z,E,E
CC conjugated triene functionality. May be involved in a stress tolerance
CC mechanism as response to intertidal habitats with direct sunlight,
CC desiccation and high temperature. In vitro substrates include
CC arachidonic acid ((5Z,8Z,11Z,14Z)-eicosatetraenoic acid), EPA ((5Z,8Z,
CC 11Z,14Z,17Z)-eicosapentaenoic acid), DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexenoic acid), adrenic acid ((7Z,10Z,13Z,16Z)-docosatetraenoic
CC acid), anandamide (arachidonyl-N-ethanolamide) and eicosatrienoic acid
CC ((5Z,8Z,11Z)-eicosatrienoic acid). Gamma-linolenic acid (18:3
CC 6Z,9Z,12Z) and dihomo-gamma-linolenic acid (20:3 8Z,11Z,14Z) are
CC transformed into mixtures of conjugated diene and triene fatty acids,
CC linoleic acid is only transformed to a conjugated diene.
CC {ECO:0000269|PubMed:12054482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate = (5Z,7E,9E,14Z,17Z)-
CC icosapentaenoate; Xref=Rhea:RHEA:14889, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:60025; EC=5.3.3.13; Evidence={ECO:0000269|PubMed:7803384,
CC ECO:0000269|PubMed:9062129};
CC -!- COFACTOR:
CC Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531;
CC Evidence={ECO:0000305|PubMed:12054482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoic acid
CC {ECO:0000269|PubMed:9062129};
CC KM=17.0 uM for (7Z,10Z,13Z,16Z)-docosatetraenoic acid
CC {ECO:0000269|PubMed:9062129};
CC KM=9.6 uM for (5Z,8Z, 11Z,14Z,17Z)-eicosapentaenoic acid
CC {ECO:0000269|PubMed:9062129};
CC KM=25.5 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
CC {ECO:0000269|PubMed:9062129};
CC KM=52.8 uM for (5Z,8Z,11Z)-eicosatrienoic acid
CC {ECO:0000269|PubMed:9062129};
CC KM=17.5 uM for arachidonyl-N-ethanolamide
CC {ECO:0000269|PubMed:9062129};
CC Vmax=1.84 umol/min/mg enzyme with (4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexenoic acid as substrate {ECO:0000269|PubMed:9062129};
CC Vmax=1.1 umol/min/mg enzyme with (7Z,10Z,13Z,16Z)-docosatetraenoic
CC acid as substrate {ECO:0000269|PubMed:9062129};
CC Vmax=6.0 umol/min/mg enzyme with (5Z,8Z, 11Z,14Z,17Z)-
CC eicosapentaenoic acid as substrate {ECO:0000269|PubMed:9062129};
CC Vmax=2.78 umol/min/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoic
CC acid as substrate {ECO:0000269|PubMed:9062129};
CC Vmax=0.31 umol/min/mg enzyme with (5Z,8Z,11Z)-eicosatrienoic acid as
CC substrate {ECO:0000269|PubMed:9062129};
CC Vmax=0.8 umol/min/mg enzyme with arachidonyl-N-ethanolamide as
CC substrate {ECO:0000269|PubMed:9062129};
CC pH dependence:
CC Optimum pH is below pH 6.0 with (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic
CC acid as substrate. {ECO:0000269|PubMed:9062129};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12054482}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12054482}.
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DR EMBL; AF354661; AAL57199.1; -; mRNA.
DR EMBL; AF354662; AAL57200.1; -; mRNA.
DR AlphaFoldDB; Q8W257; -.
DR SMR; Q8W257; -.
DR PRIDE; Q8W257; -.
DR KEGG; ag:AAL57199; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0034016; F:polyenoic fatty acid isomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12054482"
FT CHAIN 22..500
FT /note="Polyenoic fatty acid isomerase"
FT /id="PRO_0000418869"
FT CONFLICT 56..57
FT /note="ES -> SQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="G -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..328
FT /note="AD -> TN (in Ref. 1; AAL57200)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="N -> D (in Ref. 1; AAL57200)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="S -> A (in Ref. 1; AAL57200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55960 MW; F2825B6F515DBD7D CRC64;
MSLNRVLHIF LIAYLACTAL THDFDDTIAV VGAGYSGLSA AFTLVKKGYT NVEIYESQGE
VGGYVYSVDY NNVAHDLATY ALTPAYWKFQ EAMKSIGVGF CELDVAIVQT NSTPVSVPFE
KWMAAYWAAK VPNPLNLVRK VSTQVSTYVE VWKKLFNMDF IDTSTKRTNR LFPLKTNDVD
VLAQFSMPMK DFVALHKLDL LEPLFIQATD SQAYGPYDTT PALYYMVWFP PNLFNGEENT
VPCGTYNSMQ SMAEHMAEWL KSKGVTFHMN TKVTKISRAT DGSSPSLLEE GVATPKLFDT
IISTNKLPSA NRAEVVTPLL PKEREAADTY EELQMFSALL ETNRSDAIPT TGFLMVDADA
IIAHDPNTGF WGCLNAERRG GYSDENAILS SDTVTRVSAI YYYTERANNE RIDFSLDEKI
QQVKTNLATW DSATWTNLTS RTFGGYFQRW RTPDVMGQKP WNLADIQGEG DVYYVNSAAC
GFESVGHVFD CADNLIKDFF
