CKX1_MAIZE
ID CKX1_MAIZE Reviewed; 534 AA.
AC Q9T0N8; O81158;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytokinin dehydrogenase 1;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 1;
DE Short=CKO 1;
DE Short=COX 1;
DE AltName: Full=ZmCKX1;
DE Flags: Precursor;
GN Name=CKX1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 417-435; 490-517 AND
RP 524-534.
RC STRAIN=cv. Nobilis; TISSUE=Kernel;
RX PubMed=10230061; DOI=10.1046/j.1365-313x.1999.00408.x;
RA Houba-Herin N., Pethe C., D'Alayer J., Laloue M.;
RT "Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression
RT in moss protoplasts.";
RL Plant J. 17:615-626(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 286-308; 369-377;
RP 388-392 AND 417-431, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10049708; DOI=10.1006/bbrc.1999.0199;
RA Morris R.O., Bilyeu K.D., Laskey J.G., Cheikh N.N.;
RT "Isolation of a gene encoding a glycosylated cytokinin oxidase from
RT maize.";
RL Biochem. Biophys. Res. Commun. 255:328-333(1999).
RN [3]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11154345; DOI=10.1104/pp.125.1.378;
RA Bilyeu K.D., Cole J.L., Laskey J.G., Riekhof W.R., Esparza T.J.,
RA Kramer M.D., Morris R.O.;
RT "Molecular and biochemical characterization of a cytokinin oxidase from
RT maize.";
RL Plant Physiol. 125:378-386(2001).
RN [4]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=12721786; DOI=10.1007/s10265-003-0096-4;
RA Schmuelling T., Werner T., Riefler M., Krupkova E., Bartrina y Manns I.;
RT "Structure and function of cytokinin oxidase/dehydrogenase genes of maize,
RT rice, Arabidopsis and other species.";
RL J. Plant Res. 116:241-252(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-534 OF APOENZYME AND IN COMPLEX
RP WITH BENZYLAMINOPURINE; ISOPENTENYLADENINE OR TRANS-ZEATIN.
RX PubMed=15321719; DOI=10.1016/j.jmb.2004.06.083;
RA Malito E., Coda A., Bilyeu K.D., Fraaije M.W., Mattevi A.;
RT "Structures of Michaelis and product complexes of plant cytokinin
RT dehydrogenase: implications for flavoenzyme catalysis.";
RL J. Mol. Biol. 341:1237-1249(2004).
CC -!- FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)-
CC substituted adenine derivatives that are plant hormones, where the
CC substituent is an isopentenyl group. Cleaves zeatin,
CC isopentenyladenine, isopentenyladenosine, zeatin riboside and cis-
CC zeatin, but not dihydrozeatin, kinetin and benzylaminopurine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal +
CC adenine + AH2; Xref=Rhea:RHEA:13625, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15825, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17660; EC=1.5.99.12;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- ACTIVITY REGULATION: Competitive inhibition by phenylureas.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Expressed in immature kernels and unpollinated
CC cobs. Weakly expressed in kernels harvested two weeks after anthesis.
CC {ECO:0000269|PubMed:11154345}.
CC -!- PTM: Glycosylated; with approximately 10 hexose residues per site.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC 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; Y18377; CAA77151.1; -; mRNA.
DR EMBL; AF044603; AAC27500.1; -; Genomic_DNA.
DR PIR; T01500; T01500.
DR PIR; T51929; T51929.
DR RefSeq; NP_001105591.1; NM_001112121.1.
DR PDB; 1W1O; X-ray; 1.70 A; A=1-534.
DR PDB; 1W1Q; X-ray; 1.80 A; A=1-534.
DR PDB; 1W1R; X-ray; 1.90 A; A=1-534.
DR PDB; 1W1S; X-ray; 2.00 A; A=1-534.
DR PDB; 2QKN; X-ray; 2.15 A; A=19-534.
DR PDB; 2QPM; X-ray; 1.85 A; A=19-534.
DR PDB; 3BW7; X-ray; 1.95 A; A=19-534.
DR PDB; 3C0P; X-ray; 1.95 A; A=19-534.
DR PDB; 3DQ0; X-ray; 1.90 A; A=19-534.
DR PDB; 3KJM; X-ray; 1.90 A; A=19-534.
DR PDB; 3S1C; X-ray; 2.09 A; A=19-534.
DR PDB; 3S1D; X-ray; 1.75 A; A=19-534.
DR PDB; 3S1E; X-ray; 1.90 A; A=19-534.
DR PDB; 3S1F; X-ray; 2.00 A; A=19-534.
DR PDBsum; 1W1O; -.
DR PDBsum; 1W1Q; -.
DR PDBsum; 1W1R; -.
DR PDBsum; 1W1S; -.
DR PDBsum; 2QKN; -.
DR PDBsum; 2QPM; -.
DR PDBsum; 3BW7; -.
DR PDBsum; 3C0P; -.
DR PDBsum; 3DQ0; -.
DR PDBsum; 3KJM; -.
DR PDBsum; 3S1C; -.
DR PDBsum; 3S1D; -.
DR PDBsum; 3S1E; -.
DR PDBsum; 3S1F; -.
DR AlphaFoldDB; Q9T0N8; -.
DR SMR; Q9T0N8; -.
DR ChEMBL; CHEMBL5363; -.
DR PaxDb; Q9T0N8; -.
DR PRIDE; Q9T0N8; -.
DR GeneID; 542585; -.
DR KEGG; zma:542585; -.
DR MaizeGDB; 194080; -.
DR eggNOG; KOG1231; Eukaryota.
DR OrthoDB; 350817at2759; -.
DR BioCyc; MetaCyc:CKX1-MON; -.
DR BRENDA; 1.5.99.12; 6752.
DR SABIO-RK; Q9T0N8; -.
DR EvolutionaryTrace; Q9T0N8; -.
DR PRO; PR:Q9T0N8; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9T0N8; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; -; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR015345; Cytokinin_DH_FAD/cytokin-bd.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR Pfam; PF09265; Cytokin-bind; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..534
FT /note="Cytokinin dehydrogenase 1"
FT /id="PRO_0000020424"
FT DOMAIN 65..245
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 100..104
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180..184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 527..530
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Pros-8alpha-FAD histidine"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 79
FT /note="G -> A (in Ref. 1; CAA77151)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="N -> T (in Ref. 1; CAA77151)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="F -> L (in Ref. 1; CAA77151)"
FT /evidence="ECO:0000305"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1W1O"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3S1D"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 247..257
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 325..336
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:1W1O"
FT TURN 415..421
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 448..457
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 466..483
FT /evidence="ECO:0007829|PDB:1W1O"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 507..520
FT /evidence="ECO:0007829|PDB:1W1O"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:1W1O"
SQ SEQUENCE 534 AA; 57229 MW; 13FB5AF654C169E5 CRC64;
MAVVYYLLLA GLIACSHALA AGTPALGDDR GRPWPASLAA LALDGKLRTD SNATAAASTD
FGNITSALPA AVLYPSSTGD LVALLSAANS TPGWPYTIAF RGRGHSLMGQ AFAPGGVVVN
MASLGDAAAP PRINVSADGR YVDAGGEQVW IDVLRASLAR GVAPRSWNDY LYLTVGGTLS
NAGISGQAFR HGPQISNVLE MDVITGHGEM VTCSKQLNAD LFDAVLGGLG QFGVITRARI
AVEPAPARAR WVRFVYTDFA AFSADQERLT APRPGGGGAS FGPMSYVEGS VFVNQSLATD
LANTGFFTDA DVARIVALAG ERNATTVYSI EATLNYDNAT AAAAAVDQEL ASVLGTLSYV
EGFAFQRDVA YAAFLDRVHG EEVALNKLGL WRVPHPWLNM FVPRSRIADF DRGVFKGILQ
GTDIVGPLIV YPLNKSMWDD GMSAATPSED VFYAVSLLFS SVAPNDLARL QEQNRRILRF
CDLAGIQYKT YLARHTDRSD WVRHFGAAKW NRFVEMKNKY DPKRLLSPGQ DIFN
