DCYD1_ARATH
ID DCYD1_ARATH Reviewed; 401 AA.
AC F4HYF3; Q8W4C7; Q9SX74;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial;
DE EC=3.5.99.7;
DE EC=4.4.1.15;
DE AltName: Full=1-aminocyclopropane-1-carboxylic acid deaminase 1;
DE Short=AtACD1;
DE AltName: Full=AtD-CDes1;
DE Short=D-CDes1;
DE AltName: Full=D-CDES;
DE Flags: Precursor;
GN Name=DCD; Synonyms=ACD1; OrderedLocusNames=At1g48420;
GN ORFNames=F11A17.2, T1N15.3;
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] OF 2-401 AND 19-401.
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15720402; DOI=10.1111/j.1742-4658.2005.04567.x;
RA Riemenschneider A., Wegele R., Schmidt A., Papenbrock J.;
RT "Isolation and characterization of a D-cysteine desulfhydrase protein from
RT Arabidopsis thaliana.";
RL FEBS J. 272:1291-1304(2005).
RN [5]
RP FUNCTION.
RX PubMed=19508369; DOI=10.1111/j.1399-3054.2009.01208.x;
RA McDonnell L., Plett J.M., Andersson-Gunneras S., Kozela C., Dugardeyn J.,
RA Van Der Straeten D., Glick B.R., Sundberg B., Regan S.;
RT "Ethylene levels are regulated by a plant encoded 1-aminocyclopropane-1-
RT carboxylic acid deaminase.";
RL Physiol. Plantarum 136:94-109(2009).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Has high
CC affinity for D-cysteine.
CC -!- FUNCTION: Possesses 1-aminocyclopropane-1-carboxylic acid (ACC)
CC deaminase activity. Acts as a regulator of ACC levels and causes
CC changes in ethylene levels.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:11268, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35236; EC=4.4.1.15;
CC Evidence={ECO:0000269|PubMed:15720402};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC Evidence={ECO:0000269|PubMed:15720402};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15720402};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for D-cysteine {ECO:0000269|PubMed:15720402};
CC Note=kcat is 6 sec(-1) for D-cysteine as substrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15720402};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15720402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=F4HYF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HYF3-2; Sequence=VSP_057958;
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 -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 20 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49754.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL32737.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007932; AAD49754.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC020889; AAF79717.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32290.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58401.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58402.1; -; Genomic_DNA.
DR EMBL; AY062659; AAL32737.1; ALT_INIT; mRNA.
DR EMBL; AY093325; AAM13324.1; -; mRNA.
DR PIR; D96524; D96524.
DR RefSeq; NP_001319174.1; NM_001333334.1. [F4HYF3-1]
DR RefSeq; NP_001320840.1; NM_001333335.1. [F4HYF3-1]
DR RefSeq; NP_175275.3; NM_103738.7. [F4HYF3-1]
DR AlphaFoldDB; F4HYF3; -.
DR SMR; F4HYF3; -.
DR BioGRID; 26488; 1.
DR STRING; 3702.AT1G48420.1; -.
DR PaxDb; F4HYF3; -.
DR PRIDE; F4HYF3; -.
DR ProteomicsDB; 222747; -. [F4HYF3-1]
DR EnsemblPlants; AT1G48420.1; AT1G48420.1; AT1G48420. [F4HYF3-1]
DR EnsemblPlants; AT1G48420.2; AT1G48420.2; AT1G48420. [F4HYF3-1]
DR EnsemblPlants; AT1G48420.3; AT1G48420.3; AT1G48420. [F4HYF3-1]
DR GeneID; 841263; -.
DR Gramene; AT1G48420.1; AT1G48420.1; AT1G48420. [F4HYF3-1]
DR Gramene; AT1G48420.2; AT1G48420.2; AT1G48420. [F4HYF3-1]
DR Gramene; AT1G48420.3; AT1G48420.3; AT1G48420. [F4HYF3-1]
DR KEGG; ath:AT1G48420; -.
DR Araport; AT1G48420; -.
DR TAIR; locus:2007725; AT1G48420.
DR eggNOG; ENOG502QPS1; Eukaryota.
DR HOGENOM; CLU_048897_1_1_1; -.
DR InParanoid; F4HYF3; -.
DR OMA; LVQEKWV; -.
DR OrthoDB; 817780at2759; -.
DR BRENDA; 4.4.1.15; 399.
DR PRO; PR:F4HYF3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HYF3; baseline and differential.
DR Genevisible; F4HYF3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0019447; P:D-cysteine catabolic process; IDA:TAIR.
DR GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR.
DR GO; GO:1990170; P:stress response to cadmium ion; IMP:TAIR.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Hydrolase; Lyase; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..401
FT /note="Bifunctional D-cysteine desulfhydrase/1-
FT aminocyclopropane-1-carboxylate deaminase, mitochondrial"
FT /id="PRO_0000429500"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 2)"
FT /id="VSP_057958"
FT INIT_MET F4HYF3-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES F4HYF3-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 401 AA; 43900 MW; 7B2194D57373A132 CRC64;
MRGRSLTLSR VKLELARRSM SATSVPSMAD FLTKKPYSPP SWASHLRPLP SHTFSLAHLP
TPIHRWNLPG LPNGTELWIK RDDFTGMELS GNKVRKLEFL MAEAVDQHAD TVITIGGIQS
NHCRATATAS NYLNLNSHLI LRTSKLLADE DPGLVGNLLV ERLVGANVHL ISKEEYSSIG
SEALTNALKE KLEKEGKKPY VIPVGGSNSL GTWGYIEAAR EIEEQLNYRP DDLKFDDIVV
ACGSGGTIAG ISLGSWLGAL KAKVHAFSVC DDPDYFYDFV QGLLDGLHAG VNSRDIVNIH
NAKGKGYAMN TSEELEFVKK VASSTGVILD PVYSGKAAYG LINEITKDPK CWEGRKILFI
HTGGLLGLYD KVDQMASLMG NWSRMDVSES VPRKDGVGKM F
