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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
 
 
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