CNIF3_ARATH
ID CNIF3_ARATH Reviewed; 475 AA.
AC Q3E6S9; Q3E932;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Probable L-cysteine desulfhydrase, chloroplastic {ECO:0000305};
DE EC=4.4.1.-;
DE AltName: Full=Chloroplastic cysteine desulfurase-like protein 3 {ECO:0000303|PubMed:18978034};
DE AltName: Full=NIFS-like protein 3 {ECO:0000303|PubMed:18978034};
DE Short=CpNifS3 {ECO:0000303|PubMed:18978034};
DE Flags: Precursor;
GN Name=CpNIFS3 {ECO:0000303|PubMed:18978034};
GN OrderedLocusNames=At5g26600 {ECO:0000312|Araport:AT5G26600};
GN ORFNames=F21E10 {ECO:0000312|EMBL:AF058914};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
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 [4]
RP IDENTIFICATION, AND INTERACTION WITH QS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
CC -!- FUNCTION: May catalyze the production of hydrogen sulfide (H2S) from
CC cysteine. {ECO:0000250|UniProtKB:Q9M1R1}.
CC -!- SUBUNIT: Interacts in vitro with QS (PubMed:18978034).
CC {ECO:0000269|PubMed:18978034}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|RuleBase:RU004075}.
CC -!- CAUTION: Identified as a putative plastidic SufS-like protein and thus
CC called CpNifS3 (PubMed:18978034). However, it seems to be more related
CC to L-cysteine desulfhydrase. {ECO:0000303|PubMed:18978034,
CC ECO:0000305}.
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DR EMBL; AF058914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93591.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93592.1; -; Genomic_DNA.
DR EMBL; AK229365; BAF01228.1; -; mRNA.
DR RefSeq; NP_850886.1; NM_180555.3.
DR RefSeq; NP_974838.1; NM_203109.2.
DR AlphaFoldDB; Q3E6S9; -.
DR SMR; Q3E6S9; -.
DR STRING; 3702.AT5G26600.2; -.
DR PaxDb; Q3E6S9; -.
DR PRIDE; Q3E6S9; -.
DR ProteomicsDB; 220298; -.
DR EnsemblPlants; AT5G26600.1; AT5G26600.1; AT5G26600.
DR EnsemblPlants; AT5G26600.2; AT5G26600.2; AT5G26600.
DR GeneID; 832730; -.
DR Gramene; AT5G26600.1; AT5G26600.1; AT5G26600.
DR Gramene; AT5G26600.2; AT5G26600.2; AT5G26600.
DR KEGG; ath:AT5G26600; -.
DR Araport; AT5G26600; -.
DR TAIR; locus:2146829; AT5G26600.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_3_2_1; -.
DR InParanoid; Q3E6S9; -.
DR OMA; TGNCHKW; -.
DR OrthoDB; 516638at2759; -.
DR PhylomeDB; Q3E6S9; -.
DR PRO; PR:Q3E6S9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E6S9; baseline and differential.
DR Genevisible; Q3E6S9; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Chloroplast; Lyase; Plastid; Pyridoxal phosphate; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..24
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 25..475
FT /note="Probable L-cysteine desulfhydrase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432215"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9M1R1"
SQ SEQUENCE 475 AA; 52908 MW; FF5C3C30929791D4 CRC64;
MASSLSPPEE ASYHHRHTKR YTSSASSASS TTNGTVESSV SDFVKRPKIS HPNYISSSEI
ESEFSHHDPD FARINNGSFG CCPSSILALQ RDWQLRFLRQ PDRFYFDELK PKISDSRSVI
KRLINAEHDD EVSIVDNATT AAAIVLQQTA WAFREGRFDK GDAVVMLHYA YGSVKKSVEA
YVTRSGGHVT EVQLPFPVIS ADEIIDRFRI GLESGKANGR RVRLALIDHV TSMPSVVIPI
KELVKICRRE GVDQVFVDAA HGIGCVDVDM KEIGADFYTS NLHKWFFAPP SVAFLYCRKS
SNGGVADLHH PVVSNEYGNG LAVESSWVGT RDYSAQLVVP SILEFVNRFE GGIDGIKKRN
HESVVEMGQM LVKSWGTQLG CPPEMCASMI MVGLPVCLGV SSESDVLKLR TFLREKFRIE
IPIYFRPPGD GEIDPITGYV RISFQVYNKP EDYHRLRDAI NGLVRDGFKC TSLSC
