TRXF_SPIOL
ID TRXF_SPIOL Reviewed; 190 AA.
AC P09856;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Thioredoxin F-type, chloroplastic;
DE Short=Trx-F;
DE Flags: Precursor;
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], AND PROTEIN SEQUENCE OF 78-190.
RX PubMed=2737203; DOI=10.1111/j.1432-1033.1989.tb14832.x;
RA Kamo M., Tsugita A., Wiessner C., Wedel N., Bartling D., Herrmann R.G.,
RA Aguilar F., Gardet-Salvi L., Schurmann P.;
RT "Primary structure of spinach-chloroplast thioredoxin f. Protein sequencing
RT and analysis of complete cDNA clones for spinach-chloroplast thioredoxin
RT f.";
RL Eur. J. Biochem. 182:315-322(1989).
RN [2]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RX PubMed=6351859; DOI=10.1016/0006-291x(83)90960-9;
RA Tsugita A., Maeda K., Schurmann P.;
RT "Spinach chloroplast thioredoxins in evolutionary drift.";
RL Biochem. Biophys. Res. Commun. 115:1-7(1983).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 70-189, AND DISULFIDE BOND.
RX PubMed=10964566; DOI=10.1006/jmbi.2000.4006;
RA Capitani G., Markovic-Housley Z., DelVal G., Morris M., Jansonius J.N.,
RA Schurmann P.;
RT "Crystal structures of two functionally different thioredoxins in spinach
RT chloroplasts.";
RL J. Mol. Biol. 302:135-154(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 79-189 OF MUTANT SER-117 IN
RP COMPLEXES WITH BACTERIAL FTRC; FTRV AND PETF/FERREDOXIN, SUBUNIT, AND
RP MUTAGENESIS OF CYS-117.
RX PubMed=17611542; DOI=10.1038/nature05937;
RA Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P.,
RA Eklund H.;
RT "Structural snapshots along the reaction pathway of ferredoxin-thioredoxin
RT reductase.";
RL Nature 448:92-96(2007).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of the active center dithiol to a disulfide. The F
CC form is known to activate a number of enzymes of the photosynthetic
CC carbon cycle.
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and ferredoxin. {ECO:0000269|PubMed:17611542}.
CC -!- INTERACTION:
CC P09856; Q55389: ftrC; Xeno; NbExp=5; IntAct=EBI-863615, EBI-863211;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC {ECO:0000305}.
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DR EMBL; X14959; CAA33082.1; -; mRNA.
DR PIR; S04661; S04661.
DR PDB; 1F9M; X-ray; 1.86 A; A/B=78-189.
DR PDB; 1FAA; X-ray; 1.85 A; A=69-189.
DR PDB; 2PU9; X-ray; 1.65 A; C=79-189.
DR PDB; 2PVO; X-ray; 3.40 A; C=79-189.
DR PDBsum; 1F9M; -.
DR PDBsum; 1FAA; -.
DR PDBsum; 2PU9; -.
DR PDBsum; 2PVO; -.
DR AlphaFoldDB; P09856; -.
DR SMR; P09856; -.
DR DIP; DIP-37834N; -.
DR IntAct; P09856; 2.
DR SABIO-RK; P09856; -.
DR EvolutionaryTrace; P09856; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Disulfide bond;
KW Electron transport; Plastid; Redox-active center; Transit peptide;
KW Transport.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2737203"
FT CHAIN 78..190
FT /note="Thioredoxin F-type, chloroplastic"
FT /id="PRO_0000034161"
FT DOMAIN 78..189
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Nucleophile"
FT ACT_SITE 117
FT /note="Nucleophile"
FT SITE 108
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 115
FT /note="Contributes to redox potential value"
FT SITE 116
FT /note="Contributes to redox potential value"
FT DISULFID 114..117
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:10964566"
FT MUTAGEN 117
FT /note="C->S: Prevents scission of the intermolecular
FT disulfide bond by the second Cys of the active site."
FT /evidence="ECO:0000269|PubMed:17611542"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1FAA"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:1FAA"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2PU9"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2PU9"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:2PU9"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1FAA"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2PU9"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:2PU9"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2PU9"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2PVO"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:2PU9"
FT STRAND 155..175
FT /evidence="ECO:0007829|PDB:2PU9"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:2PU9"
SQ SEQUENCE 190 AA; 21024 MW; 4B162C69DBC11869 CRC64;
MALHLSLSHQ SWTSPAHPIT SSDPTRSSVP GTGLSRRVDF LGSCKINGVF VVKRKDRRRM
RGGEVRASME QALGTQEMEA IVGKVTEVNK DTFWPIVKAA GDKPVVLDMF TQWCGPCKAM
APKYEKLAEE YLDVIFLKLD CNQENKTLAK ELGIRVVPTF KILKENSVVG EVTGAKYDKL
LEAIQAARSS
