NBP35_ARATH
ID NBP35_ARATH Reviewed; 350 AA.
AC Q8H1Q2; Q9C5E1; Q9FI52;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
DE AltName: Full=Nucleotide binding protein 35;
DE Short=AtNBP35;
GN Name=NBP35 {ECO:0000255|HAMAP-Rule:MF_03038}; OrderedLocusNames=At5g50960;
GN ORFNames=K3K7.12;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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;
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 [4]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18957412; DOI=10.1074/jbc.m807303200;
RA Bych K., Netz D.J., Vigani G., Bill E., Lill R., Pierik A.J., Balk J.;
RT "The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1
RT partner in the green lineage.";
RL J. Biol. Chem. 283:35797-35804(2008).
RN [5]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF
RP CYS-28; CYS-31; CYS-322 AND CYS-328.
RX PubMed=19084504; DOI=10.1016/j.bbrc.2008.11.138;
RA Kohbushi H., Nakai Y., Kikuchi S., Yabe T., Hori H., Nakai M.;
RT "Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe-2S] and [4Fe-
RT 4S] clusters in two distinct domains.";
RL Biochem. Biophys. Res. Commun. 378:810-815(2009).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC assembly (CIA) machinery. Required for maturation of extramitochondrial
CC Fe-S proteins. Functions as Fe-S scaffold, mediating the de novo
CC assembly of an Fe-S cluster and its transfer to target apoproteins.
CC Essential for embryo development. {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:18957412, ECO:0000269|PubMed:19084504}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:18957412, ECO:0000269|PubMed:19084504};
CC Note=Binds 3 [4Fe-4S] clusters per homodimer. Contains two stable
CC clusters in the N-termini and one labile, bridging cluster between
CC subunits of the homodimer. {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:18957412, ECO:0000269|PubMed:19084504};
CC -!- SUBUNIT: Homodimer and homotetramer. Predominantly homodimeric.
CC {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:18957412,
CC ECO:0000269|PubMed:19084504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038,
CC ECO:0000269|PubMed:18957412, ECO:0000269|PubMed:19084504}.
CC -!- MISCELLANEOUS: Although plant and algal NBP35 proteins lack the
CC characteristic CXXC motif in the C-terminus, thought to be required for
CC Fe-S cluster binding, they can bind a [4Fe-4S] cluster in the C-
CC terminus. Also, in this linage, no CFD1 partner protein homolog as
CC found in other eukaryotes can be found. {ECO:0000305|PubMed:18957412}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08742.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017063; BAB08742.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96017.1; -; Genomic_DNA.
DR EMBL; AF360309; AAK26019.1; -; mRNA.
DR EMBL; AY142635; AAN13093.1; -; mRNA.
DR RefSeq; NP_568748.1; NM_124475.5.
DR AlphaFoldDB; Q8H1Q2; -.
DR SMR; Q8H1Q2; -.
DR BioGRID; 20415; 1.
DR STRING; 3702.AT5G50960.1; -.
DR iPTMnet; Q8H1Q2; -.
DR PaxDb; Q8H1Q2; -.
DR PRIDE; Q8H1Q2; -.
DR ProteomicsDB; 251250; -.
DR EnsemblPlants; AT5G50960.1; AT5G50960.1; AT5G50960.
DR GeneID; 835169; -.
DR Gramene; AT5G50960.1; AT5G50960.1; AT5G50960.
DR KEGG; ath:AT5G50960; -.
DR Araport; AT5G50960; -.
DR TAIR; locus:2157328; AT5G50960.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_0_1_1; -.
DR InParanoid; Q8H1Q2; -.
DR OMA; EMDCQVG; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q8H1Q2; -.
DR PRO; PR:Q8H1Q2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H1Q2; baseline and differential.
DR Genevisible; Q8H1Q2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03038; NUBP1; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264; PTHR23264; 1.
DR Pfam; PF10609; ParA; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..350
FT /note="Cytosolic Fe-S cluster assembly factor NBP35"
FT /id="PRO_0000421867"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT MUTAGEN 28
FT /note="C->G: Impairs [4Fe-4S] cluster binding."
FT /evidence="ECO:0000269|PubMed:19084504"
FT MUTAGEN 31
FT /note="C->G: Impairs [4Fe-4S] cluster binding."
FT /evidence="ECO:0000269|PubMed:19084504"
FT MUTAGEN 322
FT /note="C->G: Seems to promote [2Fe-2S] cluster binding in
FT the C-terminus."
FT /evidence="ECO:0000269|PubMed:19084504"
FT MUTAGEN 328
FT /note="C->G: Seems to promote [2Fe-2S] cluster binding in
FT the C-terminus."
FT /evidence="ECO:0000269|PubMed:19084504"
FT CONFLICT 343
FT /note="V -> F (in Ref. 3; AAK26019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 37306 MW; 69DD66DB069B85B8 CRC64;
MENGDIPEDA NEHCPGPQSE SAGKSDSCAG CPNQEACATA PKGPDPDLVA IAERMSTVKH
KILVLSGKGG VGKSTFSAQL SFALAGMDHQ VGLMDIDICG PSIPKMLGLE GQEIHQSNLG
WSPVYVEDNL GVMSIGFMLP NSDEAVIWRG PRKNGLIKQF LKDVYWGEID YLVVDAPPGT
SDEHISIVQY LLPTGIDGAI IVTTPQEVSL IDVRKEVSFC KKVGVPVLGV VENMSGLSQP
LKDVKFMKLA TETGSSINVT EDVIACLRKN APELLDIVAC SEVFDSSGGG AERMCREMGV
PFLGKVPMDP QLCKAAEQGK SCFEDNKCLI SAPALKSIIQ KVVPSTVMTE
