NIFU2_ARATH
ID NIFU2_ARATH Reviewed; 235 AA.
AC Q93W20; A8MS35; Q9LTX6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=NifU-like protein 2, chloroplastic;
DE Short=AtCNfu2;
DE Short=AtCnfU-V;
DE Flags: Precursor;
GN Name=NIFU2; Synonyms=CNFU2, NFU2; OrderedLocusNames=At5g49940;
GN ORFNames=K9P8.16;
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] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12553879; DOI=10.1042/bj20021946;
RA Leon S., Touraine B., Ribot C., Briat J.-F., Lobreaux S.;
RT "Iron-sulphur cluster assembly in plants: distinct NFU proteins in
RT mitochondria and plastids from Arabidopsis thaliana.";
RL Biochem. J. 371:823-830(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15031412; DOI=10.1105/tpc.020511;
RA Yabe T., Morimoto K., Kikuchi S., Nishio K., Terashima I., Nakai M.;
RT "The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an
RT iron-sulfur cluster scaffold protein, is required for biogenesis of
RT ferredoxin and photosystem I.";
RL Plant Cell 16:993-1007(2004).
RN [8]
RP FUNCTION.
RX PubMed=15361144; DOI=10.1111/j.1365-313x.2004.02189.x;
RA Touraine B., Boutin J.-P., Marion-Poll A., Briat J.-F., Peltier G.,
RA Lobreaux S.;
RT "Nfu2: a scaffold protein required for [4Fe-4S] and ferredoxin iron-sulphur
RT cluster assembly in Arabidopsis chloroplasts.";
RL Plant J. 40:101-111(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 83-235, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=18585737; DOI=10.1016/j.jmb.2008.05.072;
RA Yabe T., Yamashita E., Kikuchi A., Morimoto K., Nakagawa A., Tsukihara T.,
RA Nakai M.;
RT "Structural analysis of Arabidopsis CnfU protein: an iron-sulfur cluster
RT biosynthetic scaffold in chloroplasts.";
RL J. Mol. Biol. 381:160-173(2008).
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC chloroplastic iron-sulfur proteins. Required for biogenesis of
CC ferredoxin, a major photosynthetic electron carrier containing [2Fe-2S]
CC cluster. Required for the assembly of photosystem I complex.
CC {ECO:0000269|PubMed:15031412, ECO:0000269|PubMed:15361144}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:15031412};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:15031412};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15031412,
CC ECO:0000269|PubMed:18585737}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12553879, ECO:0000269|PubMed:15031412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93W20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93W20-2; Sequence=VSP_040522, VSP_040523;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves and floral
CC stalks. Ubiquitous (at protein level). {ECO:0000269|PubMed:12553879,
CC ECO:0000269|PubMed:15031412}.
CC -!- DISRUPTION PHENOTYPE: Plants are dwarf with faint pale-green leaves,
CC decreased amount of ferredoxin and impaired photosystem I accumulation.
CC {ECO:0000269|PubMed:15031412}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97015.1; Type=Erroneous gene model prediction; Note=The predicted gene At5g49940 has been split into 2 genes: At5g49940 and At5g49945.; Evidence={ECO:0000305};
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DR EMBL; AJ512934; CAD55559.1; -; mRNA.
DR EMBL; AB024032; BAA97015.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95873.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95874.1; -; Genomic_DNA.
DR EMBL; AK316745; BAH19468.1; -; mRNA.
DR EMBL; AF370353; AAK44168.1; -; mRNA.
DR EMBL; AF428399; AAL16167.1; -; mRNA.
DR EMBL; AY062984; AAL34158.1; -; mRNA.
DR EMBL; AK118652; BAC43248.1; -; mRNA.
DR RefSeq; NP_001078739.1; NM_001085270.2. [Q93W20-2]
DR RefSeq; NP_568715.1; NM_124372.5. [Q93W20-1]
DR PDB; 2Z51; X-ray; 1.35 A; A=83-235.
DR PDBsum; 2Z51; -.
DR AlphaFoldDB; Q93W20; -.
DR SMR; Q93W20; -.
DR BioGRID; 20303; 1.
DR STRING; 3702.AT5G49940.1; -.
DR iPTMnet; Q93W20; -.
DR PaxDb; Q93W20; -.
DR PRIDE; Q93W20; -.
DR ProteomicsDB; 251297; -. [Q93W20-1]
DR EnsemblPlants; AT5G49940.1; AT5G49940.1; AT5G49940. [Q93W20-1]
DR EnsemblPlants; AT5G49940.2; AT5G49940.2; AT5G49940. [Q93W20-2]
DR GeneID; 835057; -.
DR Gramene; AT5G49940.1; AT5G49940.1; AT5G49940. [Q93W20-1]
DR Gramene; AT5G49940.2; AT5G49940.2; AT5G49940. [Q93W20-2]
DR KEGG; ath:AT5G49940; -.
DR Araport; AT5G49940; -.
DR TAIR; locus:2158849; AT5G49940.
DR eggNOG; KOG2358; Eukaryota.
DR HOGENOM; CLU_080894_2_0_1; -.
DR InParanoid; Q93W20; -.
DR OMA; STVTMRM; -.
DR OrthoDB; 1536051at2759; -.
DR PhylomeDB; Q93W20; -.
DR EvolutionaryTrace; Q93W20; -.
DR PRO; PR:Q93W20; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93W20; baseline and differential.
DR Genevisible; Q93W20; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:TAIR.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 3.30.300.130; -; 2.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF01106; NifU; 2.
DR SUPFAM; SSF117916; SSF117916; 2.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Alternative splicing; Chloroplast; Disulfide bond;
KW Iron; Iron-sulfur; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 17..235
FT /note="NifU-like protein 2, chloroplastic"
FT /id="PRO_0000247613"
FT DISULFID 126
FT /note="Interchain (with C-129)"
FT /evidence="ECO:0000269|PubMed:18585737"
FT DISULFID 129
FT /note="Interchain (with C-126)"
FT /evidence="ECO:0000269|PubMed:18585737"
FT VAR_SEQ 175..185
FT /note="LEEIRPYLIGT -> KFWCWKKSGLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040522"
FT VAR_SEQ 186..235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040523"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2Z51"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:2Z51"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2Z51"
SQ SEQUENCE 235 AA; 25620 MW; 6443A3A407D8A3A8 CRC64;
MQLLTLNPAA ISRTPPQAID PSSSSSLLLP FPQILSSQRA LGLVARPCNP LRRGLSRFLS
SRQLFRRSKV VKAVATPDPI LEVPLTEENV ESVLDEIRPY LMSDGGNVAL HEIDGNIVRV
KLQGACGSCP SSTMTMKMGI ERRLMEKIPE IVAVEALPDE ETGLELNEEN IEKVLEEIRP
YLIGTADGSL DLVEIEDPIV KIRITGPAAG VMTVRVAVTQ KLREKIPSIA AVQLI
