FER_PHYPA
ID FER_PHYPA Reviewed; 145 AA.
AC O04166; A9SZY5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferredoxin, chloroplastic;
DE Flags: Precursor;
GN Name=PETF; ORFNames=PHYPADRAFT_190267, PHYPADRAFT_190462;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kleber-Janke T., Wehe M., Kruse S., Reski R.;
RT "Transcriptional analysis of ferredoxin from a moss.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; Y12734; CAA73265.1; -; mRNA.
DR EMBL; DS545032; EDQ63350.1; -; Genomic_DNA.
DR EMBL; DS545035; EDQ63083.1; -; Genomic_DNA.
DR RefSeq; XP_001771921.1; XM_001771869.1.
DR RefSeq; XP_001772139.1; XM_001772087.1.
DR AlphaFoldDB; O04166; -.
DR SMR; O04166; -.
DR STRING; 3218.PP1S143_176V6.1; -.
DR EnsemblPlants; Pp3c4_8159V3.1; PAC:32919644.CDS.1; Pp3c4_8159.
DR EnsemblPlants; Pp3c4_8330V3.1; PAC:32919949.CDS.1; Pp3c4_8330.
DR EnsemblPlants; Pp3c4_8330V3.2; PAC:32919950.CDS.1; Pp3c4_8330.
DR Gramene; Pp3c4_8159V3.1; PAC:32919644.CDS.1; Pp3c4_8159.
DR Gramene; Pp3c4_8330V3.1; PAC:32919949.CDS.1; Pp3c4_8330.
DR Gramene; Pp3c4_8330V3.2; PAC:32919950.CDS.1; Pp3c4_8330.
DR eggNOG; ENOG502S3RJ; Eukaryota.
DR HOGENOM; CLU_082632_1_1_1; -.
DR OMA; KITCMAT; -.
DR OrthoDB; 1557921at2759; -.
DR Proteomes; UP000006727; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript level;
KW 2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 49..145
FT /note="Ferredoxin, chloroplastic"
FT /id="PRO_0000008837"
FT DOMAIN 51..143
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 94
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 145 AA; 15217 MW; D37C7BE216629C82 CRC64;
MAAAAMTSIV PVASIAPVSK VANVRPSSVS VAKAFGLKSR SMGRLTCMAT YKVTFLDGET
GAENVVECSD EEYVLDAAER AGMDLPYSCR AGACSSCAGI IKAGEVDQSD QSFLDDSQID
DGFVLTCVAY PASDCIILTH QEENM
