MGL_ARATH
ID MGL_ARATH Reviewed; 441 AA.
AC Q9SGU9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Methionine gamma-lyase;
DE Short=AtMGL;
DE EC=4.4.1.11;
DE AltName: Full=L-methioninase;
GN Name=MGL; OrderedLocusNames=At1g64660; ORFNames=F1N19.23;
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=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=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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY HIGH
RP MET LEVELS, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=17030798; DOI=10.1073/pnas.0606195103;
RA Rebeille F., Jabrin S., Bligny R., Loizeau K., Gambonnet B., Van Wilder V.,
RA Douce R., Ravanel S.;
RT "Methionine catabolism in Arabidopsis cells is initiated by a gamma-
RT cleavage process and leads to S-methylcysteine and isoleucine syntheses.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15687-15692(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP INDUCTION BY SULFATE DEPRIVATION, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=17169919; DOI=10.1093/pcp/pcl055;
RA Goyer A., Collakova E., Shachar-Hill Y., Hanson A.D.;
RT "Functional characterization of a methionine gamma-lyase in Arabidopsis and
RT its implication in an alternative to the reverse trans-sulfuration
RT pathway.";
RL Plant Cell Physiol. 48:232-242(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY DROUGHT.
RC STRAIN=cv. Columbia;
RX PubMed=19571310; DOI=10.1104/pp.109.138651;
RA Joshi V., Jander G.;
RT "Arabidopsis methionine gamma-lyase is regulated according to isoleucine
RT biosynthesis needs but plays a subordinate role to threonine deaminase.";
RL Plant Physiol. 151:367-378(2009).
CC -!- FUNCTION: Catalyzes the degradation of L-methionine to alpha-
CC ketobutyrate, methanethiol and ammonia. Exhibits a high activity toward
CC L-methionine, L-ethionine, L-homocysteine and seleno-L-methionine, but
CC not L-cysteine. Involved in an alternative cysteine biosynthesis
CC pathway to the reverse trans-sulfuration pathway
CC (methionine->homocysteine->cystathionine->cysteine) in which
CC methanethiol is an intermediate. Mediates also an alternative
CC isoleucine biosynthesis pathway in which 2-ketobutyrate is an
CC intermediate. {ECO:0000269|PubMed:17169919,
CC ECO:0000269|PubMed:19571310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+);
CC Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11;
CC Evidence={ECO:0000269|PubMed:17030798, ECO:0000269|PubMed:17169919};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=422 nm {ECO:0000269|PubMed:17030798,
CC ECO:0000269|PubMed:17169919};
CC Kinetic parameters:
CC KM=10 mM for L-methionine (at pH 7.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17030798};
CC KM=72 mM for L-methionine (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17169919};
CC KM=14 mM for L-ethionine (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17169919};
CC KM=92 mM for L-homocysteine (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17169919};
CC KM=40 mM for seleno-L-methionine (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17169919};
CC Vmax=194 nmol/min/mg enzyme with L-methionine as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:17169919};
CC Vmax=182 nmol/min/mg enzyme with L-ethionine as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:17169919};
CC Vmax=743 nmol/min/mg enzyme with L-homocysteine as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:17169919};
CC Vmax=238 nmol/min/mg enzyme with seleno-L-methionine as substrate (at
CC pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:17169919};
CC Note=kcat is 9.5 sec(-1) with L-methionine as substrate, 8.9 sec(-1)
CC with L-ethionine as substrate, 36.2 sec(-1) with L-homocysteine as
CC substrate and 11.6 sec(-1) with seleno-L-methionine as substrate
CC (PubMed:17169919, at pH 8 and 30 degrees Celsius).;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17169919}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17030798}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, siliques, leaves,
CC flowers and seeds after imbibition (at protein level). Transcripts
CC accumulate in dry mature seeds, but at protein level, only present upon
CC imbibition. {ECO:0000269|PubMed:17030798, ECO:0000269|PubMed:17169919}.
CC -!- INDUCTION: By sulfate deprivation and high methionine levels. Up-
CC regulated by drought. {ECO:0000269|PubMed:17030798,
CC ECO:0000269|PubMed:17169919, ECO:0000269|PubMed:19571310}.
CC -!- DISRUPTION PHENOTYPE: Increased leaves, flowers and seeds methionine
CC content, and leaf and root S-methylmethionine content under conditions
CC of sulfate starvation. Reduced MGL-mediated isoleucine biosynthesis
CC from methionine. {ECO:0000269|PubMed:17169919,
CC ECO:0000269|PubMed:19571310}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AC009519; AAF19680.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34271.1; -; Genomic_DNA.
DR EMBL; AF428413; AAL16181.1; -; mRNA.
DR EMBL; AY054546; AAK96737.1; -; mRNA.
DR EMBL; BT006588; AAP31932.1; -; mRNA.
DR EMBL; AK226375; BAE98522.1; -; mRNA.
DR PIR; G96669; G96669.
DR RefSeq; NP_176647.1; NM_105141.3.
DR AlphaFoldDB; Q9SGU9; -.
DR SMR; Q9SGU9; -.
DR STRING; 3702.AT1G64660.1; -.
DR PaxDb; Q9SGU9; -.
DR PRIDE; Q9SGU9; -.
DR ProteomicsDB; 238895; -.
DR EnsemblPlants; AT1G64660.1; AT1G64660.1; AT1G64660.
DR GeneID; 842774; -.
DR Gramene; AT1G64660.1; AT1G64660.1; AT1G64660.
DR KEGG; ath:AT1G64660; -.
DR Araport; AT1G64660; -.
DR TAIR; locus:2019449; AT1G64660.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_0_1; -.
DR InParanoid; Q9SGU9; -.
DR OMA; FNAWVLS; -.
DR OrthoDB; 572061at2759; -.
DR PhylomeDB; Q9SGU9; -.
DR BioCyc; ARA:AT1G64660-MON; -.
DR BioCyc; MetaCyc:AT1G64660-MON; -.
DR BRENDA; 4.4.1.11; 399.
DR PRO; PR:Q9SGU9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGU9; baseline and differential.
DR Genevisible; Q9SGU9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0018826; F:methionine gamma-lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP:UniProtKB.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0019458; P:methionine catabolic process via 2-oxobutanoate; TAS:TAIR.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..441
FT /note="Methionine gamma-lyase"
FT /id="PRO_0000420159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 47821 MW; 8CF2025201571FA1 CRC64;
MAHFLETQEP LVFSGKKRND RDDEDGDALV AKKSALAVCD ADPAAAIANI RHEFGEHGGV
NMSIEASATF TVMEPDTMRR MFTGELGPDN DFYVYSRHFN PTVLNLSRQM AALEGTQAAY
CTSSGMSAIS SVMLQLCSSG GHVVAASTLY GGTHALLSHF LPRTCNITTS FVDITDHGAV
ANAIVEGRTQ VLYFESVANP TLTVADIPEL SRMAHEKGVT VVVDNTFAPM VLSPAKLGAD
VVVHSISKFI SGGADIIAGA VCGSENLVKE MMDLRGGSLM LLGPTMNAKV AFELSERIPH
LGLRMREHSH RAQVYAERMR DLGMKVIYPG LETHPQHKLF KGMVNRDYGY GGLLSIDMET
EEKANKLMAY LQNATQFGFM AVSLGYYETL MSCSGSSTSS ELDPSQKEAA GISPGLVRMS
VGYVGTLEQK WTQFEKAFLR M
