TRXM_PEA
ID TRXM_PEA Reviewed; 172 AA.
AC P48384; Q40992;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Thioredoxin M-type, chloroplastic;
DE Short=Trx-M;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Green leaf;
RX PubMed=8058831; DOI=10.1104/pp.105.3.1021;
RA Lopez Jaramillo J., Chueca A., Sahrawy M., Hermoso R., Lazaro J.J.,
RA Prado F.E., Lopez Gorge J.;
RT "Cloning and sequencing of a pea cDNA fragment coding for thioredoxin m.";
RL Plant Physiol. 105:1021-1022(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8642611; DOI=10.1007/bf02498636;
RA Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.;
RT "Intron position as an evolutionary marker of thioredoxins and thioredoxin
RT domains.";
RL J. Mol. Evol. 42:422-431(1996).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and ferredoxin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
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DR EMBL; X76269; CAA53900.1; -; mRNA.
DR EMBL; U35831; AAC49358.1; -; Genomic_DNA.
DR PIR; S38909; S38909.
DR AlphaFoldDB; P48384; -.
DR SMR; P48384; -.
DR PRIDE; P48384; -.
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 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; Electron transport; Plastid;
KW Redox-active center; Transit peptide; Transport.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..172
FT /note="Thioredoxin M-type, chloroplastic"
FT /id="PRO_0000034177"
FT DOMAIN 61..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 98
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 99
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 97..100
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 30
FT /note="L -> F (in Ref. 2; AAC49358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19156 MW; 991F519C4B32B09A CRC64;
MALESLFKSI HTKTSLSSSI VFIFKGKACL LTSKSRIQES FAELNSFTSL VLLIENHVLL
HAREAVNEVQ VVNDSSWDEL VIGSETPVLV DFWAPWCGPC RMIAPIIDEL AKEYAGKIKC
YKLNTDESPN TATKYGIRSI PTVLFFKNGE RKDSVIGAVP KATLSEKVEK YI
