ID   LCYD1_ARATH             Reviewed;         454 AA.
AC   Q9M1R1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=L-cysteine desulfhydrase;
DE            EC=4.4.1.28;
DE   AltName: Full=AtL-CDes1;
DE            Short=L-CDes1;
DE   AltName: Full=AtLCD;
GN   Name=LCD; OrderedLocusNames=At3g62130; ORFNames=T17J13.90;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY DROUGHT.
RX   PubMed=21986537; DOI=10.1016/j.bbrc.2011.09.090;
RA   Jin Z., Shen J., Qiao Z., Yang G., Wang R., Pei Y.;
RT   "Hydrogen sulfide improves drought resistance in Arabidopsis thaliana.";
RL   Biochem. Biophys. Res. Commun. 414:481-486(2011).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23178483; DOI=10.1016/j.plaphy.2012.10.017;
RA   Jin Z., Xue S., Luo Y., Tian B., Fang H., Li H., Pei Y.;
RT   "Hydrogen sulfide interacting with abscisic acid in stomatal regulation
RT   responses to drought stress in Arabidopsis.";
RL   Plant Physiol. Biochem. 62:41-46(2013).
CC   -!- FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from
CC       cysteine. Is mainly responsible for the degradation of cysteine to
CC       generate H2S, a regulator of stomatal movement and closure.
CC       {ECO:0000269|PubMed:21986537, ECO:0000269|PubMed:23178483}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:35235; EC=4.4.1.28;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Highly expressed in stems and cauline leaves, and
CC       at lower levels in roots, rosette leaves and flowers.
CC       {ECO:0000269|PubMed:21986537}.
CC   -!- INDUCTION: By drought. {ECO:0000269|PubMed:21986537}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have enlarged stomatal aperture and
CC       increased sensitivity to drought stress. {ECO:0000269|PubMed:23178483}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase 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; AL138651; CAB71873.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80314.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65747.1; -; Genomic_DNA.
DR   EMBL; AY062517; AAL32595.1; -; mRNA.
DR   EMBL; BT008756; AAP49518.1; -; mRNA.
DR   EMBL; AY086807; AAM63856.1; -; mRNA.
DR   PIR; T48005; T48005.
DR   RefSeq; NP_001327694.1; NM_001340141.1.
DR   RefSeq; NP_191772.1; NM_116078.4.
DR   AlphaFoldDB; Q9M1R1; -.
DR   SMR; Q9M1R1; -.
DR   STRING; 3702.AT3G62130.1; -.
DR   PaxDb; Q9M1R1; -.
DR   PRIDE; Q9M1R1; -.
DR   ProteomicsDB; 238412; -.
DR   EnsemblPlants; AT3G62130.1; AT3G62130.1; AT3G62130.
DR   EnsemblPlants; AT3G62130.2; AT3G62130.2; AT3G62130.
DR   GeneID; 825386; -.
DR   Gramene; AT3G62130.1; AT3G62130.1; AT3G62130.
DR   Gramene; AT3G62130.2; AT3G62130.2; AT3G62130.
DR   KEGG; ath:AT3G62130; -.
DR   Araport; AT3G62130; -.
DR   TAIR; locus:2098068; AT3G62130.
DR   eggNOG; KOG1549; Eukaryota.
DR   HOGENOM; CLU_003433_3_2_1; -.
DR   InParanoid; Q9M1R1; -.
DR   OMA; LRVYHAI; -.
DR   OrthoDB; 516638at2759; -.
DR   PhylomeDB; Q9M1R1; -.
DR   BRENDA; 4.4.1.1; 399.
DR   PRO; PR:Q9M1R1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1R1; baseline and differential.
DR   Genevisible; Q9M1R1; AT.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IDA:TAIR.
DR   GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IDA:TAIR.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome; Stress response.
FT   CHAIN           1..454
FT                   /note="L-cysteine desulfhydrase"
FT                   /id="PRO_0000429504"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         257
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  50692 MW;  E65633E8BB619B25 CRC64;
     MEAGERRNGD SMSHNHRAPK KPRLAGLLTE SDIDSEFAHH QTGVARINNG SFGCCPGSVL
     EAQREWQLRY LRQPDEFYFN GLRRGLLASR TVISDLINAD DVDEVSLVDN ATTAAAIVLQ
     KVGRCFSEGK YKKEDTVVMF HCAFQSVKKS IQAYVSRVGG STVEVRLPFP VNSNEEIISK
     FREGLEKGRA NGRTVRLAII DHITSMPCVL MPVRELVKIC REEGVEQVFV DAAHAIGSVK
     VDVKEIGADY YVSNLHKWFF CPPSIAFFYC KKRGSESDVH HPVVSHEFGN GLPIESAWIG
     TRDYSSQLVV PSVMEFVNRF EGGMEGIMMK NHDEAVRMGL MLADAWGTNL GSPPEMCVGM
     VMIGLPSKLC VGSDEDAIKL RSYLRVHYSV EVPVFYLGLR DGEEGVKDKD SGLITAYVRI
     SHQVYNKTED YERLRDAITE LVKDQMTCQN LPAL