DCYD2_ARATH
ID DCYD2_ARATH Reviewed; 427 AA.
AC A1L4V7; Q0WQC8; Q9LJG2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=D-cysteine desulfhydrase 2, mitochondrial;
DE EC=4.4.1.15;
DE AltName: Full=AtD-CDes1;
DE Short=D-CDes1;
DE Flags: Precursor;
GN OrderedLocusNames=At3g26115; ORFNames=MPE11.30;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RA Riemenschneider A.;
RT "Isolation and characterization of cysteine degrading and H2S-releasing
RT proteins in higher plants.";
RL Thesis (2006), University of Hannover, Germany.
CC -!- FUNCTION: Catalyzes the production of hydrogen sulfide (H2S) from
CC cysteine. Can accept both D-cysteine and L-cysteine as substrate.
CC {ECO:0000269|Ref.6}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1L4V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1L4V7-2; Sequence=VSP_054966;
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000601; BAB01437.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB023041; BAB01437.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77120.1; -; Genomic_DNA.
DR EMBL; AK228771; BAF00671.1; -; mRNA.
DR EMBL; BT029744; ABM06014.1; -; mRNA.
DR RefSeq; NP_189241.3; NM_113517.4. [A1L4V7-1]
DR AlphaFoldDB; A1L4V7; -.
DR SMR; A1L4V7; -.
DR STRING; 3702.AT3G26115.2; -.
DR iPTMnet; A1L4V7; -.
DR PaxDb; A1L4V7; -.
DR PRIDE; A1L4V7; -.
DR ProteomicsDB; 222748; -. [A1L4V7-1]
DR EnsemblPlants; AT3G26115.1; AT3G26115.1; AT3G26115. [A1L4V7-1]
DR GeneID; 822210; -.
DR Gramene; AT3G26115.1; AT3G26115.1; AT3G26115. [A1L4V7-1]
DR KEGG; ath:AT3G26115; -.
DR Araport; AT3G26115; -.
DR TAIR; locus:2090345; AT3G26115.
DR eggNOG; ENOG502QPSP; Eukaryota.
DR OMA; WEVYAVM; -.
DR OrthoDB; 730428at2759; -.
DR PRO; PR:A1L4V7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A1L4V7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; TAS:UniProtKB.
DR GO; GO:0009093; P:cysteine catabolic process; TAS:UniProtKB.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lyase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..427
FT /note="D-cysteine desulfhydrase 2, mitochondrial"
FT /id="PRO_0000429501"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 353
FT /note="K -> NSFCSCR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_054966"
SQ SEQUENCE 427 AA; 47430 MW; 76A9A689D00C5826 CRC64;
MKVQRSTFLA VTGKSNLHHF HSSSQRIPIT SEIDSREFVS KLLDRKWGLQ CPASPIQQIS
VSSVKGIDKF SFLNNTRPHL GDEMSKSKQG SSFYILRDDL LHPLVNGNKA RKLDALLPLV
EDHKVTDLVT CGGCQSAHTA AVAVSCAERG LRSHLLLRGE QPDVLTGYNL VSTMYGNVQY
VPRSRYANRE EMLRTYADLV AGEDGTVLWA KDIVEGRDTM NVAKMDDFSS MKTSRRKVLI
VNEGAGDALA LLGMFRLVQH LSQDHLLGKK RPVKFVVDAG TGTTAVGLGV AAMSLGLPWE
INAVMLADTL KNYKRHEDHL IAEFSRQFPG SVFCSGLDMN QMIKWIDRQH PRKFGKVLEG
EVEMCRKIAQ ETGVLVDPMY TLAAWETATE LVQDEKSSIV VMLHTGGTLG MFGLAQRYKT
CFTNLKD
