MDLL_ARATH
ID MDLL_ARATH Reviewed; 552 AA.
AC Q9SSM2; Q1PFE0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=(R)-mandelonitrile lyase-like;
DE EC=4.1.2.10;
DE AltName: Full=Hydroxynitrile lyase-like;
DE Short=(R)-oxynitrilase-like;
DE Flags: Precursor;
GN OrderedLocusNames=At1g73050; ORFNames=F3N23.25;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mandelonitrile = benzaldehyde + hydrogen cyanide;
CC Xref=Rhea:RHEA:18313, ChEBI:CHEBI:17169, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:18450; EC=4.1.2.10;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AC008017; AAD55652.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35408.1; -; Genomic_DNA.
DR EMBL; DQ446423; ABE65766.1; -; mRNA.
DR PIR; A96756; A96756.
DR RefSeq; NP_177448.1; NM_105963.1.
DR AlphaFoldDB; Q9SSM2; -.
DR SMR; Q9SSM2; -.
DR STRING; 3702.AT1G73050.1; -.
DR PaxDb; Q9SSM2; -.
DR PRIDE; Q9SSM2; -.
DR ProteomicsDB; 228870; -.
DR EnsemblPlants; AT1G73050.1; AT1G73050.1; AT1G73050.
DR GeneID; 843636; -.
DR Gramene; AT1G73050.1; AT1G73050.1; AT1G73050.
DR KEGG; ath:AT1G73050; -.
DR Araport; AT1G73050; -.
DR TAIR; locus:2032642; AT1G73050.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_026750_0_0_1; -.
DR InParanoid; Q9SSM2; -.
DR OMA; NEGVGYF; -.
DR OrthoDB; 798314at2759; -.
DR PhylomeDB; Q9SSM2; -.
DR BioCyc; ARA:AT1G73050-MON; -.
DR PRO; PR:Q9SSM2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSM2; baseline and differential.
DR Genevisible; Q9SSM2; AT.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046593; F:mandelonitrile lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Lyase; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..552
FT /note="(R)-mandelonitrile lyase-like"
FT /id="PRO_0000412562"
FT ACT_SITE 492
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 55..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
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 257
FT /note="G -> R (in Ref. 3; ABE65766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 60783 MW; 7747A5D5C2DA7C7A CRC64;
MTKRIDSSLL YTALVVLLLL GVVHRSNARP RVNRPPGFMR FISNATDFAS EDYYDYIIVG
GGTAGCPLAA TLSQSFRVLL LERGGVPYNR PNVMSHDGFL TTLTDVNNFD SPAQSFISEE
GVPNARGRVL GGSSAINAGF YSRADKQFFE NSGLVWDLSS VNQSYEWVER AIVFRPQLRT
WQTAIRDALL EVGVHPFNGF TLEHKVGTKI GGSTFDRTGR RHSSADLLRY ARSSNIRVAV
YATVERVLLA SSPSVSGSNV SAIGVVYRDQ LGRFHHALIR DRGEVILSAG ALGSPQLLFL
SGIGPRSYLS TWGIPVALDQ PHVGDFVYDN PRNGISIVPP VPMENSLIQV VGVTEDGAFL
EAASNVIPFA SPLHSVFIRA PASPLYVPVT TIMEKILGPV SIGLLRLAST DVRINPVVRF
NYFSDPQDLE RCVNGTRKIG EILRSRAMQD FMIREWFGNR RFRFVGAPLP VDQSNDLVMA
DFCRRTVSTI WHYHGGAVVG KVVDSDLKVI GVNSLRLVDG STFNISPGTN PQATLMMLGR
YMGLKMLRER MR
