ID   MAX1_ARATH              Reviewed;         522 AA.
AC   B9DFU2; O64853; Q940L3;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Cytochrome P450 711A1 {ECO:0000303|PubMed:15737939};
DE            EC=1.14.-.- {ECO:0000269|PubMed:25425668};
DE   AltName: Full=Protein MORE AXILLARY BRANCHES 1 {ECO:0000303|PubMed:15737939};
GN   Name=CYP711A1 {ECO:0000303|PubMed:15737939};
GN   Synonyms=MAX1 {ECO:0000303|PubMed:15737939};
GN   OrderedLocusNames=At2g26170 {ECO:0000312|Araport:AT2G26170};
GN   ORFNames=T19L18.2 {ECO:0000312|EMBL:AAM15001.1}, T1D16.2
GN   {ECO:0000312|EMBL:AAC14532.2};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15737939; DOI=10.1016/j.devcel.2005.01.009;
RA   Booker J., Sieberer T., Wright W., Williamson L., Willett B., Stirnberg P.,
RA   Turnbull C., Srinivasan M., Goddard P., Leyser O.;
RT   "MAX1 encodes a cytochrome P450 family member that acts downstream of
RT   MAX3/4 to produce a carotenoid-derived branch-inhibiting hormone.";
RL   Dev. Cell 8:443-449(2005).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16387852; DOI=10.1073/pnas.0509463102;
RA   Lazar G., Goodman H.M.;
RT   "MAX1, a regulator of the flavonoid pathway, controls vegetative axillary
RT   bud outgrowth in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:472-476(2006).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20667910; DOI=10.1242/dev.051987;
RA   Crawford S., Shinohara N., Sieberer T., Williamson L., George G.,
RA   Hepworth J., Mueller D., Domagalska M.A., Leyser O.;
RT   "Strigolactones enhance competition between shoot branches by dampening
RT   auxin transport.";
RL   Development 137:2905-2913(2010).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21119045; DOI=10.1104/pp.110.164640;
RA   Kohlen W., Charnikhova T., Liu Q., Bours R., Domagalska M.A., Beguerie S.,
RA   Verstappen F., Leyser O., Bouwmeester H., Ruyter-Spira C.;
RT   "Strigolactones are transported through the xylem and play a key role in
RT   shoot architectural response to phosphate deficiency in nonarbuscular
RT   mycorrhizal host Arabidopsis.";
RL   Plant Physiol. 155:974-987(2011).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23204501; DOI=10.1093/mp/sss138;
RA   Fukui K., Ito S., Asami T.;
RT   "Selective mimics of strigolactone actions and their potential use for
RT   controlling damage caused by root parasitic weeds.";
RL   Mol. Plant 6:88-99(2013).
RN   [11]
RP   FUNCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX   PubMed=25425668; DOI=10.1073/pnas.1410801111;
RA   Abe S., Sado A., Tanaka K., Kisugi T., Asami K., Ota S., Kim H.I.,
RA   Yoneyama K., Xie X., Ohnishi T., Seto Y., Yamaguchi S., Akiyama K.,
RA   Yoneyama K., Nomura T.;
RT   "Carlactone is converted to carlactonoic acid by MAX1 in Arabidopsis and
RT   its methyl ester can directly interact with AtD14 in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:18084-18089(2014).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija-4;
RX   PubMed=27194725; DOI=10.1073/pnas.1601729113;
RA   Brewer P.B., Yoneyama K., Filardo F., Meyers E., Scaffidi A., Frickey T.,
RA   Akiyama K., Seto Y., Dun E.A., Cremer J.E., Kerr S.C., Waters M.T.,
RA   Flematti G.R., Mason M.G., Weiller G., Yamaguchi S., Nomura T., Smith S.M.,
RA   Yoneyama K., Beveridge C.A.;
RT   "LATERAL BRANCHING OXIDOREDUCTASE acts in the final stages of strigolactone
RT   biosynthesis in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:6301-6306(2016).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=32399509; DOI=10.1002/pld3.219;
RA   Yoneyama K., Akiyama K., Brewer P.B., Mori N., Kawano-Kawada M., Haruta S.,
RA   Nishiwaki H., Yamauchi S., Xie X., Umehara M., Beveridge C.A., Yoneyama K.,
RA   Nomura T.;
RT   "Hydroxyl carlactone derivatives are predominant strigolactones in
RT   Arabidopsis.";
RL   Plant Direct 4:e00219-e00219(2020).
CC   -!- FUNCTION: Involved in the biosynthesis of strigolactone natural
CC       products, bioactive compounds promoting plant fitness and soil microbe
CC       interactions, but preventing shoot branching (PubMed:25425668,
CC       PubMed:32399509). Converts carlactone to carlactonoic acid by
CC       catalyzing consecutive oxidations at C-19 to convert the C-19 methyl
CC       group into carboxylic acid (PubMed:25425668). Prefers 11R-carlactone to
CC       11S-carlactone as substrate (PubMed:25425668). Acts downstream of
CC       CCD7/MAX3 and CCD8/MAX4 in strigolactone signaling pathway and may be
CC       implicated in synthesis of carotenoid-derived branch regulators. Acts
CC       as a positive regulator of the flavonoid pathway in the late vegetative
CC       stage plant. Strigolactones are hormones that inhibit tillering and
CC       shoot branching through the MAX-dependent pathway, contribute to the
CC       regulation of shoot architectural response to phosphate-limiting
CC       conditions and function as rhizosphere signal that stimulates hyphal
CC       branching of arbuscular mycorrhizal fungi and trigger seed germination
CC       of root parasitic weeds (PubMed:15737939, PubMed:16387852).
CC       {ECO:0000269|PubMed:15737939, ECO:0000269|PubMed:16387852,
CC       ECO:0000269|PubMed:25425668, ECO:0000269|PubMed:32399509}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R)-carlactone + reduced [NADPH--hemoprotein reductase] + O2
CC         = (11R)-19-hydroxycarlactone + oxidized [NADPH--hemoprotein
CC         reductase] + H2O + H(+); Xref=Rhea:RHEA:76083, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:194508, ChEBI:CHEBI:194510;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76084;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R)-19-hydroxycarlactone + reduced [NADPH--hemoprotein
CC         reductase] + O2 = (11R)-19-oxocarlactone + oxidized
CC         [NADPH--hemoprotein reductase] + 2 H2O + H(+); Xref=Rhea:RHEA:76091,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:194510, ChEBI:CHEBI:194511;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76092;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R)-19-oxocarlactone + reduced [NADPH--hemoprotein
CC         reductase] + O2 = (11R)-carlactonoate + oxidized [NADPH--hemoprotein
CC         reductase] + H2O + 2 H(+); Xref=Rhea:RHEA:76095, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:194504, ChEBI:CHEBI:194511;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76096;
CC         Evidence={ECO:0000269|PubMed:25425668};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B9DFU2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B9DFU2-2; Sequence=VSP_046323;
CC   -!- TISSUE SPECIFICITY: Expressed in the vascular cylinder (including the
CC       pericycle) in roots, the cambial region of vascular bundles in
CC       inflorescence stems and the vascular junctions of axillary regions in
CC       leaves and flowers. {ECO:0000269|PubMed:15737939}.
CC   -!- DISRUPTION PHENOTYPE: Increased shoot branching (PubMed:15737939,
CC       PubMed:16387852, PubMed:20667910, PubMed:21119045, PubMed:23204501).
CC       Accumulation of 3-hydroxycarlactone (3-HO-CL), 4-hydroxycarlactone (4-
CC       HO-CL) and 16-hydroxycarlactone (16-HO-CL) but not of their expected
CC       corresponding metabolites hydroxycarlactonoate (HO-CLAs)
CC       (PubMed:32399509). {ECO:0000269|PubMed:15737939,
CC       ECO:0000269|PubMed:16387852, ECO:0000269|PubMed:20667910,
CC       ECO:0000269|PubMed:21119045, ECO:0000269|PubMed:23204501,
CC       ECO:0000269|PubMed:32399509}.
CC   -!- MISCELLANEOUS: The branching phenotypes of the max1, ccd7/max3 and
CC       ccd8/max4 mutants can be rescued by exogenous treatment with the
CC       synthetic strigolactone analogs GR24 and 4BD (Probable). However, the
CC       max1 mutant does not respond to carlactone (CL) (Probable).
CC       {ECO:0000305|PubMed:23204501, ECO:0000305|PubMed:27194725}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL91286.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC004484; AAC14532.2; -; Genomic_DNA.
DR   EMBL; AC004747; AAM15001.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07803.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07804.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7036392.1; -; Genomic_DNA.
DR   EMBL; AY054283; AAL06942.1; -; mRNA.
DR   EMBL; AY090384; AAL91286.1; ALT_FRAME; mRNA.
DR   EMBL; AK316903; BAH19609.1; -; mRNA.
DR   PIR; T02607; T02607.
DR   RefSeq; NP_565617.2; NM_128175.3. [B9DFU2-1]
DR   RefSeq; NP_850074.1; NM_179743.2. [B9DFU2-2]
DR   AlphaFoldDB; B9DFU2; -.
DR   SMR; B9DFU2; -.
DR   BioGRID; 2509; 1.
DR   FunCoup; B9DFU2; 476.
DR   STRING; 3702.B9DFU2; -.
DR   GlyGen; B9DFU2; 1 site.
DR   iPTMnet; B9DFU2; -.
DR   PaxDb; 3702-B9DFU2; -.
DR   ProteomicsDB; 238685; -. [B9DFU2-1]
DR   GeneID; 817157; -.
DR   KEGG; ath:AT2G26170; -.
DR   Araport; AT2G26170; -.
DR   TAIR; AT2G26170; CYP711A1.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; B9DFU2; -.
DR   OMA; WKRHGVK; -.
DR   PhylomeDB; B9DFU2; -.
DR   PRO; PR:B9DFU2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; B9DFU2; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; TAS:TAIR.
DR   GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IEP:TAIR.
DR   GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR   GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR   FunFam; 1.10.630.10:FF:000152; Cytochrome P450 711A1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24301; THROMBOXANE-A SYNTHASE; 1.
DR   PANTHER; PTHR24301:SF2; THROMBOXANE-A SYNTHASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Cytochrome P450 711A1"
FT                   /id="PRO_0000422062"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         467
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|UniProtKB:P04798"
FT   VAR_SEQ         1..83
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_046323"
SQ   SEQUENCE   522 AA;  59425 MW;  77E46CD65838398F CRC64;
     MKTQHQWWEV LDPFLTQHEA LIAFLTFAAV VIVIYLYRPS WSVCNVPGPT AMPLVGHLPL
     MAKYGPDVFS VLAKQYGPIF RFQMGRQPLI IIAEAELCRE VGIKKFKDLP NRSIPSPISA
     SPLHKKGLFF TRDKRWSKMR NTILSLYQPS HLTSLIPTMH SFITSATHNL DSKPRDIVFS
     NLFLKLTTDI IGQAAFGVDF GLSGKKPIKD VEVTDFINQH VYSTTQLKMD LSGSLSIILG
     LLIPILQEPF RQVLKRIPGT MDWRVEKTNA RLSGQLNEIV SKRAKEAETD SKDFLSLILK
     ARESDPFAKN IFTSDYISAV TYEHLLAGSA TTAFTLSSVL YLVSGHLDVE KRLLQEIDGF
     GNRDLIPTAH DLQHKFPYLD QVIKEAMRFY MVSPLVARET AKEVEIGGYL LPKGTWVWLA
     LGVLAKDPKN FPEPEKFKPE RFDPNGEEEK HRHPYAFIPF GIGPRACVGQ RFALQEIKLT
     LLHLYRNYIF RHSLEMEIPL QLDYGIILSF KNGVKLRTIK RF
//