FER2_MAIZE
ID FER2_MAIZE Reviewed; 140 AA.
AC O80429; B6UC73;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ferredoxin-2, chloroplastic {ECO:0000303|Ref.2};
DE AltName: Full=Ferredoxin II {ECO:0000303|PubMed:9952443};
DE Short=Fd II {ECO:0000303|PubMed:9952443};
DE Flags: Precursor;
GN Name=FDX2 {ECO:0000303|Ref.2}; Synonyms=pFD2 {ECO:0000303|PubMed:9952443};
GN ORFNames=GRMZM2G048313 {ECO:0000305};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-109,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Golden cross Bantam T51;
RX PubMed=9952443; DOI=10.1104/pp.119.2.481;
RA Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T., Murata H.,
RA Takao T., Shimonishi Y., Hase T.;
RT "Complementary DNA cloning and characterization of ferredoxin localized in
RT bundle-sheath cells of maize leaves.";
RL Plant Physiol. 119:481-488(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng Y., Liu Z., Fan Z.;
RT "Chloroplast precursor of maize ferredoxin 2 (Fd II).";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [6]
RP PROTEIN SEQUENCE OF 45-64.
RX PubMed=16668188; DOI=10.1104/pp.96.1.77;
RA Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.;
RT "Molecular cloning and differential expression of the maize ferredoxin gene
RT family.";
RL Plant Physiol. 96:77-83(1991).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. Occupies a key position both
CC for transferring the photoreducing power to Fd-NADP(+) oxidoreductase
CC (FNR), hence the formation of NADPH, and for mediating the cyclic
CC electron flow around photosystem I (PSI). {ECO:0000269|PubMed:9952443}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -406 mV. {ECO:0000269|PubMed:9952443};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9952443}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in bundle-sheath.
CC {ECO:0000269|PubMed:9952443}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AB016810; BAA32348.1; -; mRNA.
DR EMBL; EU328186; ACA34368.1; -; mRNA.
DR EMBL; BT039722; ACF84727.1; -; mRNA.
DR EMBL; EU974838; ACG46956.1; -; mRNA.
DR PIR; T01170; T01170.
DR RefSeq; NP_001104844.1; NM_001111374.1.
DR AlphaFoldDB; O80429; -.
DR SMR; O80429; -.
DR STRING; 4577.GRMZM2G048313_P01; -.
DR PaxDb; O80429; -.
DR PRIDE; O80429; -.
DR EnsemblPlants; Zm00001eb260160_T001; Zm00001eb260160_P001; Zm00001eb260160.
DR GeneID; 541619; -.
DR Gramene; Zm00001eb260160_T001; Zm00001eb260160_P001; Zm00001eb260160.
DR KEGG; zma:541619; -.
DR MaizeGDB; 66392; -.
DR eggNOG; ENOG502S3RJ; Eukaryota.
DR HOGENOM; CLU_082632_1_1_1; -.
DR OMA; AYPRSNC; -.
DR OrthoDB; 1557921at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; O80429; baseline and differential.
DR Genevisible; O80429; ZM.
DR GO; GO:0009507; C:chloroplast; TAS:AgBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; TAS:AgBase.
DR GO; GO:0009416; P:response to light stimulus; TAS:AgBase.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16668188"
FT CHAIN 45..140
FT /note="Ferredoxin-2, chloroplastic"
FT /id="PRO_0000433609"
FT DOMAIN 47..137
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MUTAGEN 109
FT /note="N->D: Increased affinity for Fd-NADP(+)
FT oxidoreductase and increased electron-transfer activity."
FT /evidence="ECO:0000269|PubMed:9952443"
FT CONFLICT 58
FT /note="V -> M (in Ref. 5; ACG46956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 15086 MW; 9808821CD48372A3 CRC64;
MAATALSMSI LRAPPPCFSS PLRLRVAVAK PLAAPMRRQL LRAQATYNVK LITPEGEVEL
QVPDDVYILD FAEEEGIDLP FSCRAGSCSS CAGKVVSGSV DQSDQSFLND NQVADGWVLT
CAAYPTSDVV IETHKEDDLL
