TRXM_SPIOL
ID TRXM_SPIOL Reviewed; 181 AA.
AC P07591; Q41394; Q41395;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Thioredoxin M-type, chloroplastic;
DE Short=Trx-M;
DE Contains:
DE RecName: Full=Thioredoxin M-type Mc;
DE Contains:
DE RecName: Full=Thioredoxin M-type Md;
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].
RX PubMed=1536927; DOI=10.1007/bf00040668;
RA Wedel N., Clausmeyer S., Herrmann R.G., Gardet-Salvi L., Schurmann P.;
RT "Nucleotide sequence of cDNAs encoding the entire precursor polypeptide for
RT thioredoxin m from spinach chloroplasts.";
RL Plant Mol. Biol. 18:527-533(1992).
RN [2]
RP PROTEIN SEQUENCE OF 68-181.
RX PubMed=3510868; DOI=10.1111/j.1432-1033.1986.tb09379.x;
RA Maeda K., Tsugita A., Dalzoppo D., Vilbois F., Schurmann P.;
RT "Further characterization and amino acid sequence of m-type thioredoxins
RT from spinach chloroplasts.";
RL Eur. J. Biochem. 154:197-203(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 75-179, 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 (3.00 ANGSTROMS) OF 75-180 OF MUTANT SER-107 IN
RP COMPLEXES WITH BACTERIAL FTRC; FTRV AND PETF/FERREDOXIN, SUBUNIT, AND
RP MUTAGENESIS OF CYS-107.
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 M
CC form is known to activate NADP-malate dehydrogenase.
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and ferredoxin. {ECO:0000269|PubMed:17611542}.
CC -!- INTERACTION:
CC P07591; Q55389: ftrC; Xeno; NbExp=4; IntAct=EBI-537449, EBI-863211;
CC P07591; Q9LU86: PRXQ; Xeno; NbExp=2; IntAct=EBI-537449, EBI-540311;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51462; CAA35826.1; -; mRNA.
DR EMBL; X51463; CAA35827.1; -; mRNA.
DR PIR; S20496; TXSPM.
DR PDB; 1FB0; X-ray; 2.26 A; A/B=75-179.
DR PDB; 1FB6; X-ray; 2.10 A; A/B=75-179.
DR PDB; 1GL8; NMR; -; A=76-179.
DR PDB; 2PUK; X-ray; 3.00 A; C/G=75-180.
DR PDBsum; 1FB0; -.
DR PDBsum; 1FB6; -.
DR PDBsum; 1GL8; -.
DR PDBsum; 2PUK; -.
DR AlphaFoldDB; P07591; -.
DR SMR; P07591; -.
DR DIP; DIP-33500N; -.
DR IntAct; P07591; 43.
DR OrthoDB; 1482186at2759; -.
DR SABIO-RK; P07591; -.
DR EvolutionaryTrace; P07591; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR InterPro; IPR005746; Thioredoxin.
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 TIGRFAMs; TIGR01068; thioredoxin; 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..67
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:3510868"
FT CHAIN 68..181
FT /note="Thioredoxin M-type, chloroplastic"
FT /id="PRO_0000034178"
FT CHAIN 69..181
FT /note="Thioredoxin M-type Mc"
FT /id="PRO_0000045891"
FT CHAIN 70..181
FT /note="Thioredoxin M-type Md"
FT /id="PRO_0000045892"
FT DOMAIN 68..180
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 104
FT /note="Nucleophile"
FT ACT_SITE 107
FT /note="Nucleophile"
FT SITE 98
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 105
FT /note="Contributes to redox potential value"
FT SITE 106
FT /note="Contributes to redox potential value"
FT DISULFID 104..107
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:10964566"
FT VARIANT 25
FT /note="H -> Y"
FT VARIANT 33
FT /note="V -> L"
FT VARIANT 37
FT /note="T -> S"
FT MUTAGEN 107
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 CONFLICT 83
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..95
FT /note="ESEVPV -> QSSEPS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="Y -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..170
FT /note="AVPKST -> DVSKYQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1FB6"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1FB6"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1FB6"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1GL8"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1FB6"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1GL8"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:1FB6"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1FB6"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1FB6"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1FB6"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:1FB6"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:1FB6"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1FB6"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:1FB6"
SQ SEQUENCE 181 AA; 19840 MW; 5127D4BDF72D81E9 CRC64;
MAIENCLQLS TSASVGTVAV KSHVHHLQPS SKVNVPTFRG LKRSFPALSS SVSSSSPRQF
RYSSVVCKAS EAVKEVQDVN DSSWKEFVLE SEVPVMVDFW APWCGPCKLI APVIDELAKE
YSGKIAVYKL NTDEAPGIAT QYNIRSIPTV LFFKNGERKE SIIGAVPKST LTDSIEKYLS
P
