MNIF1_ARATH
ID MNIF1_ARATH Reviewed; 453 AA.
AC O49543;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cysteine desulfurase, mitochondrial;
DE EC=2.8.1.7;
DE AltName: Full=NIFS homolog 1 {ECO:0000303|Ref.1};
DE Short=AtNIFS1;
DE AltName: Full=Protein AtMtNifS;
DE Flags: Precursor;
GN Name=NIFS1 {ECO:0000303|Ref.1};
GN Synonyms=MtNIFS1, NIFS, NSF1 {ECO:0000303|PubMed:17417719};
GN OrderedLocusNames=At5g65720 {ECO:0000312|Araport:AT5G65720};
GN ORFNames=F6H11.150 {ECO:0000312|EMBL:CAA16686.1},
GN MPA24.7 {ECO:0000312|EMBL:BAB10679.1};
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 [MRNA].
RA Burandt P., Schmidt A., Papenbrock J.;
RT "Isolation and characterization of a nifS-like protein from Arabidopsis
RT thaliana.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Picciocchi A., Alban C.;
RT "Cysteine desulfurase from A. thaliana.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP FUNCTION, INTERACTION WITH SUFE1, AND ACTIVITY REGULATION.
RX PubMed=16437155; DOI=10.1038/sj.emboj.7600968;
RA Xu X.M., Moeller S.G.;
RT "AtSufE is an essential activator of plastidic and mitochondrial
RT desulfurases in Arabidopsis.";
RL EMBO J. 25:900-909(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17417719; DOI=10.1007/s11103-007-9147-x;
RA Frazzon A.P.G., Ramirez M.V., Warek U., Balk J., Frazzon J., Dean D.R.,
RA Winkel B.S.J.;
RT "Functional analysis of Arabidopsis genes involved in mitochondrial iron-
RT sulfur cluster assembly.";
RL Plant Mol. Biol. 64:225-240(2007).
RN [10]
RP 3D-STRUCTURE MODELING, COFACTOR, INTERACTION WITH FH, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=22511606; DOI=10.1093/mp/sss037;
RA Turowski V.R., Busi M.V., Gomez-Casati D.F.;
RT "Structural and functional studies of the mitochondrial cysteine
RT desulfurase from Arabidopsis thaliana.";
RL Mol. Plant 5:1001-1010(2012).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC produce alanine. Supplies the inorganic sulfur for iron-sulfur (Fe-S)
CC clusters. {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:17417719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000269|PubMed:17417719};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22511606};
CC -!- ACTIVITY REGULATION: Threefold increase in the catalytic activity in
CC the presence of FH (frataxin) (PubMed:22511606). 30-fold increase in
CC the catalytic activity in the presence of SUFE1 (PubMed:16437155).
CC {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:22511606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=21.2 nmol/min/mg enzyme with cysteine as substrate
CC {ECO:0000269|PubMed:22511606};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000303|PubMed:17417719};
CC -!- SUBUNIT: Interacts with FH (PubMed:22511606). Interacts with SUFE1
CC (PubMed:16437155). {ECO:0000269|PubMed:16437155,
CC ECO:0000269|PubMed:22511606}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:17417719}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O49543-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:17417719}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; AJ243393; CAB64727.1; -; mRNA.
DR EMBL; AF229854; AAK00758.1; -; mRNA.
DR EMBL; AB010075; BAB10679.1; -; Genomic_DNA.
DR EMBL; AL021684; CAA16686.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98094.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68565.1; -; Genomic_DNA.
DR EMBL; AY050874; AAK92811.1; -; mRNA.
DR EMBL; AY096358; AAM19999.1; -; mRNA.
DR PIR; T05896; T05896.
DR RefSeq; NP_001318886.1; NM_001345717.1. [O49543-1]
DR RefSeq; NP_201373.1; NM_125969.3. [O49543-1]
DR AlphaFoldDB; O49543; -.
DR SMR; O49543; -.
DR BioGRID; 21943; 2.
DR IntAct; O49543; 1.
DR STRING; 3702.AT5G65720.1; -.
DR MetOSite; O49543; -.
DR PaxDb; O49543; -.
DR PRIDE; O49543; -.
DR EnsemblPlants; AT5G65720.1; AT5G65720.1; AT5G65720. [O49543-1]
DR EnsemblPlants; AT5G65720.3; AT5G65720.3; AT5G65720. [O49543-1]
DR GeneID; 836701; -.
DR Gramene; AT5G65720.1; AT5G65720.1; AT5G65720. [O49543-1]
DR Gramene; AT5G65720.3; AT5G65720.3; AT5G65720. [O49543-1]
DR KEGG; ath:AT5G65720; -.
DR Araport; AT5G65720; -.
DR TAIR; locus:2169985; AT5G65720.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_0_2_1; -.
DR InParanoid; O49543; -.
DR OMA; APHIINF; -.
DR PhylomeDB; O49543; -.
DR BRENDA; 2.8.1.6; 399.
DR BRENDA; 2.8.1.7; 399.
DR SABIO-RK; O49543; -.
DR PRO; PR:O49543; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O49543; baseline and differential.
DR Genevisible; O49543; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:TAIR.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02006; IscS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..453
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000001299"
FT ACT_SITE 377
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 123..124
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 203
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 231
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 251..253
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 291
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 377
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /note="via persulfide group"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT MOD_RES 254
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 453 AA; 50296 MW; 9BA6987AE45F09AE CRC64;
MASKVISATI RRTLTKPHGT FSRCRYLSTA AAATEVNYED ESIMMKGVRI SGRPLYLDMQ
ATTPIDPRVF DAMNASQIHE YGNPHSRTHL YGWEAENAVE NARNQVAKLI EASPKEIVFV
SGATEANNMA VKGVMHFYKD TKKHVITTQT EHKCVLDSCR HLQQEGFEVT YLPVKTDGLV
DLEMLREAIR PDTGLVSIMA VNNEIGVVQP MEEIGMICKE HNVPFHTDAA QAIGKIPVDV
KKWNVALMSM SAHKIYGPKG VGALYVRRRP RIRLEPLMNG GGQERGLRSG TGATQQIVGF
GAACELAMKE MEYDEKWIKG LQERLLNGVR EKLDGVVVNG SMDSRYVGNL NLSFAYVEGE
SLLMGLKEVA VSSGSACTSA SLEPSYVLRA LGVDEDMAHT SIRFGIGRFT TKEEIDKAVE
LTVKQVEKLR EMSPLYEMVK EGIDIKNIQW SQH