C77A4_ARATH
ID C77A4_ARATH Reviewed; 512 AA.
AC Q9LZ31; Q8L9A1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome P450 77A4;
DE EC=1.14.-.-;
DE AltName: Full=Fatty acid epoxidase;
GN Name=CYP77A4; OrderedLocusNames=At5g04660; ORFNames=T1E3.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=19120447; DOI=10.1111/j.1742-4658.2008.06819.x;
RA Sauveplane V., Kandel S., Kastner P.E., Ehlting J., Compagnon V.,
RA Werck-Reichhart D., Pinot F.;
RT "Arabidopsis thaliana CYP77A4 is the first cytochrome P450 able to catalyze
RT the epoxidation of free fatty acids in plants.";
RL FEBS J. 276:719-735(2009).
CC -!- FUNCTION: Catalyzes the epoxidation of physiological unsaturated fatty
CC acids in vitro. Can use laurate, oleate, linoleate, linolenate and
CC vernolate as substrate. {ECO:0000269|PubMed:19120447}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL162972; CAB86008.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90769.1; -; Genomic_DNA.
DR EMBL; AY088562; AAM66094.1; -; mRNA.
DR PIR; T48462; T48462.
DR RefSeq; NP_196086.1; NM_120548.3.
DR AlphaFoldDB; Q9LZ31; -.
DR SMR; Q9LZ31; -.
DR STRING; 3702.AT5G04660.1; -.
DR PaxDb; Q9LZ31; -.
DR PRIDE; Q9LZ31; -.
DR ProteomicsDB; 239201; -.
DR EnsemblPlants; AT5G04660.1; AT5G04660.1; AT5G04660.
DR GeneID; 830343; -.
DR Gramene; AT5G04660.1; AT5G04660.1; AT5G04660.
DR KEGG; ath:AT5G04660; -.
DR Araport; AT5G04660; -.
DR TAIR; locus:2180213; AT5G04660.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9LZ31; -.
DR OMA; RIHANVY; -.
DR PhylomeDB; Q9LZ31; -.
DR BioCyc; ARA:MON-16208; -.
DR BioCyc; MetaCyc:AT5G04660-MON; -.
DR PRO; PR:Q9LZ31; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZ31; differential.
DR Genevisible; Q9LZ31; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Cytochrome P450 77A4"
FT /id="PRO_0000411196"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 456
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="F -> S (in Ref. 3; AAM66094)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="S -> T (in Ref. 3; AAM66094)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="E -> D (in Ref. 3; AAM66094)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="I -> V (in Ref. 3; AAM66094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58138 MW; 30A1E94A0E8F6B3F CRC64;
MFPLISFSPT SLDFTFFAII ISGFVFIITR WNSNSKKRLN LPPGPPGWPV VGNLFQFARS
GKPFFEYAED LKKTYGPIFT LRMGTRTMII LSDATLVHEA LIQRGALFAS RPAENPTRTI
FSCNKFTVNA AKYGPVWRSL RRNMVQNMLS STRLKEFGKL RQSAMDKLIE RIKSEARDND
GLIWVLKNAR FAAFCILLEM CFGIEMDEET IEKMDEILKT VLMTVDPRID DYLPILAPFF
SKERKRALEV RREQVDYVVG VIERRRRAIQ NPGSDKTASS FSYLDTLFDL KIEGRKTTPS
NEELVTLCSE FLNGGTDTTG TAIEWGIAQL IANPEIQSRL YDEIKSTVGD DRRVDEKDVD
KMVFLQAFVK ELLRKHPPTY FSLTHAVMET TTLAGYDIPA GVNVEVYLPG ISEDPRIWNN
PKKFDPDRFM LGKEDADITG ISGVKMIPFG VGRRICPGLA MATIHVHLML ARMVQEFEWC
AHPPGSEIDF AGKLEFTVVM KNPLRAMVKP RI
