FAO3_ARATH
ID FAO3_ARATH Reviewed; 746 AA.
AC Q9LW56; Q8LGV0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Long-chain-alcohol oxidase FAO3;
DE EC=1.1.3.20;
DE AltName: Full=Long-chain fatty alcohol oxidase 3;
GN Name=FAO3; OrderedLocusNames=At3g23410; ORFNames=MLM24.14, MLM24.23;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-746, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15358540; DOI=10.1016/j.febslet.2004.07.086;
RA Cheng Q., Liu H.T., Bombelli P., Smith A., Slabas A.R.;
RT "Functional identification of AtFao3, a membrane bound long chain alcohol
RT oxidase in Arabidopsis thaliana.";
RL FEBS Lett. 574:62-68(2004).
RN [5]
RP IDENTIFICATION.
RX PubMed=10660617; DOI=10.1074/jbc.275.6.4445;
RA Vanhanen S., West M., Kroon J.T., Lindner N., Casey J., Cheng Q.,
RA Elborough K.M., Slabas A.R.;
RT "A consensus sequence for long-chain fatty-acid alcohol oxidases from
RT Candida identifies a family of genes involved in lipid omega-oxidation in
RT yeast with homologues in plants and bacteria.";
RL J. Biol. Chem. 275:4445-4452(2000).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18396913; DOI=10.1021/bp0703533;
RA Zhao S., Lin Z., Ma W., Luo D., Cheng Q.;
RT "Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in
RT lotus japonicus.";
RL Biotechnol. Prog. 24:773-779(2008).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation. {ECO:0000269|PubMed:15358540,
CC ECO:0000269|PubMed:18396913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC Evidence={ECO:0000269|PubMed:18396913};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.8 uM for 1-dodecanol {ECO:0000269|PubMed:18396913};
CC KM=680 uM for 1-hexadecanol {ECO:0000269|PubMed:18396913};
CC KM=245 uM for 1,16-hexadecandiol {ECO:0000269|PubMed:18396913};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15358540}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB015474; BAB02285.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76762.1; -; Genomic_DNA.
DR EMBL; AF361827; AAK32839.1; -; mRNA.
DR EMBL; BT002713; AAO11629.1; -; mRNA.
DR EMBL; AJ316230; CAC87643.1; -; mRNA.
DR RefSeq; NP_001325678.1; NM_001338634.1.
DR RefSeq; NP_566729.1; NM_113244.3.
DR AlphaFoldDB; Q9LW56; -.
DR SMR; Q9LW56; -.
DR BioGRID; 7254; 20.
DR IntAct; Q9LW56; 18.
DR STRING; 3702.AT3G23410.1; -.
DR PaxDb; Q9LW56; -.
DR PRIDE; Q9LW56; -.
DR ProteomicsDB; 230850; -.
DR EnsemblPlants; AT3G23410.1; AT3G23410.1; AT3G23410.
DR GeneID; 821922; -.
DR Gramene; AT3G23410.1; AT3G23410.1; AT3G23410.
DR KEGG; ath:AT3G23410; -.
DR Araport; AT3G23410; -.
DR TAIR; locus:2090900; AT3G23410.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_1_1; -.
DR InParanoid; Q9LW56; -.
DR OrthoDB; 626762at2759; -.
DR PhylomeDB; Q9LW56; -.
DR BioCyc; ARA:AT3G23410-MON; -.
DR BioCyc; MetaCyc:AT3G23410-MON; -.
DR SABIO-RK; Q9LW56; -.
DR PRO; PR:Q9LW56; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW56; baseline and differential.
DR Genevisible; Q9LW56; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IDA:UniProtKB.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012400; Long_Oxdase.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF028937; Lg_Ch_AO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..746
FT /note="Long-chain-alcohol oxidase FAO3"
FT /id="PRO_0000395504"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 677
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 233..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 746 AA; 81389 MW; 6C9C90D1CD48D9EB CRC64;
MDKYKVAGKF GLPDITVAEM ESLASFCEAV LPSVQPPPEE LSGEGDNHRN KEALRSFYST
SGSKTPVLRQ SIELVTKRGT IEAYIATRLI LFLLATRLGT LLICGTECLV SRWPFVEKFS
ELSLEKRERV LQKQFKNWIL TPIRAAFVYI KVAFLFCFFS RVNPNGENPA WEAIGYRVNP
DENKPSETHN ERPLEKGIVE TMEETEQTLL ESLAHKGLEA VLDTEHDAIR IKCDVVVVGS
GSGGGVAASV LAKSGLKVVV LEKGSYFTPS EHRPFEGPGL DKLYENGGIL PSVDGSFMVL
AGATVGGGSA VNWSACIKTP KSVLQEWSED QNIPLFGTKE YLTAMEVVWK RMGVTEKCEL
ESFQNQILRK GCENLGFNVE NVPRNSSESH YCGSCGYGCR QGDKKGSDRT WLVDAVGHGA
VILTGCKAER FILEKNGSNK GGKQMKCLGV MAKSLNGNIA KMLKIEAKVT VSAGGALLTP
PLMISSGLRN RNIGKNLHLH PVLMAWGYFP DKESSNISFK GNSYEGGIIT SVSKVLSEDS
EVRAIIETPQ LGPGSFSVLT PWTSGLDMKK RMARYSRTAS LITIVRDRGS GEVKTEGRIN
YTVDKTDRDN LKAGLRESLR ILIAAGAEEV GTHRSDGQRL ICKGVNENSI QEFLDSVSTE
EGAKGMTEKW NVYSSAHQMG SCRIGENEKE GAIDLNGESW EAEKLFVCDA SALPSAVGVN
PMITVMSTAY CISTRIAKSM TTGLSH
