FTRV_SPIOL
ID FTRV_SPIOL Reviewed; 174 AA.
AC P38365;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Ferredoxin-thioredoxin reductase, variable chain, chloroplastic;
DE Short=FTR-V;
DE AltName: Full=Ferredoxin-thioredoxin reductase subunit A;
DE Short=FTR-A;
DE Flags: Precursor;
GN Name=FTRV;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gaymard E., Schuermann P.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Green leaf;
RX PubMed=8167141; DOI=10.1016/0005-2728(94)90218-6;
RA Falkenstein E., von Schaewen A., Scheibe R.;
RT "Full-length cDNA sequences for both ferredoxin-thioredoxin reductase
RT subunits from spinach (Spinacia oleracea L.).";
RL Biochim. Biophys. Acta 1185:252-254(1994).
RN [3]
RP PROTEIN SEQUENCE OF 63-174.
RC TISSUE=Leaf;
RX PubMed=8055915; DOI=10.1111/j.1432-1033.1994.tb19014.x;
RA Iwadate H., Yano K., Kamo M., Gardet-Salvi L., Schuermann P., Tsugita A.;
RT "Amino acid sequence of spinach ferredoxin:thioredoxin reductase variable
RT subunit.";
RL Eur. J. Biochem. 223:465-471(1994).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND PHOSPHORYLATION AT SER-70 AND SER-71.
RX PubMed=1924273;
RA Tsugita A., Yano K., Gardet-Salvi L., Schuermann P.;
RT "Characterization of spinach ferredoxin-thioredoxin reductase.";
RL Protein Seq. Data Anal. 4:9-13(1991).
CC -!- FUNCTION: Variable subunit of the ferredoxin-thioredoxin reductase
CC (FTR), which catalyzes the two-electron reduction of thioredoxins by
CC the electrons provided by reduced ferredoxin.
CC -!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit B
CC (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin
CC and thioredoxin.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the ferredoxin thioredoxin reductase alpha
CC subunit family. {ECO:0000305}.
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DR EMBL; X78880; CAA55480.1; -; mRNA.
DR EMBL; X77162; CAA54407.1; -; mRNA.
DR EMBL; X77163; CAA54408.1; -; mRNA.
DR PIR; S44200; RDSPTA.
DR AlphaFoldDB; P38365; -.
DR SMR; P38365; -.
DR iPTMnet; P38365; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:InterPro.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR004207; Fd_thioredoxin_Rdtase_alpha.
DR InterPro; IPR044166; FTRV.
DR PANTHER; PTHR46937; PTHR46937; 1.
DR Pfam; PF02941; FeThRed_A; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Oxidoreductase; Phosphoprotein;
KW Plastid; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1924273,
FT ECO:0000269|PubMed:8055915"
FT CHAIN 63..174
FT /note="Ferredoxin-thioredoxin reductase, variable chain,
FT chloroplastic"
FT /id="PRO_0000021290"
FT REGION 69..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1924273,
FT ECO:0000269|PubMed:8055915"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1924273,
FT ECO:0000269|PubMed:8055915"
FT VARIANT 56
FT /note="A -> E (in A2)"
FT VARIANT 80
FT /note="S -> SS (in A2)"
SQ SEQUENCE 174 AA; 19075 MW; BE1F06D460B521F5 CRC64;
MTTGVAVMSS ATAASTATAT AAATARIPLF LSRNNSSATV CSTLRCRTIT RTRTRARLAI
CCEVALKSDS STGFDSSSSS PPEEDEELKK NLEKVGCKVK VKSPLKVYHV PKLPEVELTP
DMVGVIKQYV GFWKGKYISP NYPFKVEYRI DVPDRGSVKL VVHLKEEEFE IIAE