FAO4A_ARATH
ID FAO4A_ARATH Reviewed; 726 AA.
AC O65709;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Long-chain-alcohol oxidase FAO4A;
DE EC=1.1.3.20;
DE AltName: Full=Long-chain fatty alcohol oxidase 4A;
GN Name=FAO4A; OrderedLocusNames=At4g19380; ORFNames=T5K18.160;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78940.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022580; CAA18625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78940.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84174.1; -; Genomic_DNA.
DR PIR; T05821; T05821.
DR RefSeq; NP_193673.2; NM_118058.3.
DR AlphaFoldDB; O65709; -.
DR SMR; O65709; -.
DR BioGRID; 12972; 6.
DR IntAct; O65709; 6.
DR STRING; 3702.AT4G19380.1; -.
DR PaxDb; O65709; -.
DR PRIDE; O65709; -.
DR EnsemblPlants; AT4G19380.1; AT4G19380.1; AT4G19380.
DR GeneID; 827679; -.
DR Gramene; AT4G19380.1; AT4G19380.1; AT4G19380.
DR KEGG; ath:AT4G19380; -.
DR Araport; AT4G19380; -.
DR TAIR; locus:2140401; AT4G19380.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_0_1; -.
DR InParanoid; O65709; -.
DR PhylomeDB; O65709; -.
DR PRO; PR:O65709; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65709; baseline and differential.
DR Genevisible; O65709; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..726
FT /note="Long-chain-alcohol oxidase FAO4A"
FT /id="PRO_0000395505"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 659
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 224..239
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 726 AA; 80068 MW; 65EFDA4E670DF876 CRC64;
MESLVAICDT FISSIDDSGV GHVDDCVAGY FSASASQTGT PDRVARLMSE RLHHPKKWIL
RAGLWLLSTW IGSLVLCGWR SFTGEFPYFR RFCRLPEKRR EEILLNWSSS YFSLLRMLFR
TIKLISALVF FTQVDEKGRN LAWKAIGYNG PSPDHSDHEV ELNEEKKKKK PEEIFGPLYN
GIVDLKSPRE AVEKKLAGRG FAVSNQKRNT NGSSISDPVM KIQCDAVVVG SGSGGGVAAG
VLAKAGYKVL VIESGNYYAR SKLSLLEGQA MDDMYLSGGL LATSDTNVVI LAGSTVGGGS
TINWSASIKT PEHVMKEWAE KSKLEMFGSD LYREAMDVVC KRMGVQCGFV EEGFNNEVLR
KGCEKLGLPV KNIPRNAPSD HYCGFCCLGC KKGQKQGTSE TWLVDLVESD NGLILPGCQA
TEVMYDCEQG KKKKATGVAF AFGEEIYVVE SRVTIVACGA LRTPHLLKRS GLKNSNIGRN
LCLHPVVMAW GWFPEEDKWP EKKKKSYEGG IMTAMSSVVI EETHSSYGEM VIQTPALHPG
MFSGIIPWTS SKDFKTRMLK FSRTAHIFAL LRDKGTGTID SKTYIDYNLN DEDEESLKNG
LERVLKILAA AGAEEIGTHH SEGRSLNVRT ASSLEIERFV REESSKPLKD LSGQICSAHQ
MGSCRMGIRP EESAVRPTGE TWEVERLFVA DTSVFPTALG VNPMVTVQSI AYCIGLNVVD
VLKKKK