TRXM_CHLRE
ID TRXM_CHLRE Reviewed; 140 AA.
AC P23400;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Thioredoxin M-type, chloroplastic;
DE Short=Trx-M;
DE AltName: Full=Thioredoxin-CH2;
DE Flags: Precursor;
GN Name=TRXM;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7632918; DOI=10.1007/bf00020396;
RA Stein M., Jacquot J.-P., Jeannette E., Decottignies P., Hodges M.,
RA Lancelin J.-M., Mittard V., Schmitter J.-M., Miginiac-Maslow M.;
RT "Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for
RT the chloroplastic m and cytosolic h isoforms; expression in Escherichia
RT coli of the recombinant proteins, purification and biochemical
RT properties.";
RL Plant Mol. Biol. 28:487-503(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-140.
RX PubMed=1741302; DOI=10.1093/nar/20.3.617;
RA Jacquot J.-P., Stein M., Hodges M., Miginiac-Maslow M.;
RT "PCR cloning of a nucleotidic sequence coding for the mature part of
RT Chlamydomonas reinhardtii thioredoxin Ch2.";
RL Nucleic Acids Res. 20:617-617(1992).
RN [3]
RP PROTEIN SEQUENCE OF 35-140, AND DISULFIDE BOND.
RC STRAIN=137c / CC-125;
RX PubMed=2191628; DOI=10.1016/0003-9861(90)90525-4;
RA Decottignies P., Schmitter J.-M., Jacquot J.-P., Dutka S., Picaud A.,
RA Gadal P.;
RT "Purification, characterization, and complete amino acid sequence of a
RT thioredoxin from a green alga, Chlamydomonas reinhardtii.";
RL Arch. Biochem. Biophys. 280:112-121(1990).
RN [4]
RP STRUCTURE BY NMR.
RA Lancelin J.-M., Guilhaudis L., Krimm I., Blackledge M.J., Marion D.,
RA Jacquot J.-P.;
RT "NMR structure and dynamic of the chloroplast thioredoxin M CH2 from the
RT green alga Chlamydomonas reinhardtii.";
RL Submitted (NOV-1999) to the PDB data bank.
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; X80888; CAA56851.1; -; Genomic_DNA.
DR EMBL; X78821; CAA55398.1; -; mRNA.
DR EMBL; X62335; CAA44209.1; -; mRNA.
DR PIR; S57774; S57774.
DR RefSeq; XP_001690314.1; XM_001690262.1.
DR PDB; 1DBY; NMR; -; A=35-140.
DR PDBsum; 1DBY; -.
DR AlphaFoldDB; P23400; -.
DR SMR; P23400; -.
DR STRING; 3055.EDP10052; -.
DR ProMEX; P23400; -.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_2_1; -.
DR OMA; YKNNKEW; -.
DR OrthoDB; 1482186at2759; -.
DR EvolutionaryTrace; P23400; -.
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..34
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2191628"
FT CHAIN 35..140
FT /note="Thioredoxin M-type, chloroplastic"
FT /id="PRO_0000034174"
FT DOMAIN 35..140
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 64
FT /note="Nucleophile"
FT ACT_SITE 67
FT /note="Nucleophile"
FT SITE 58
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 65
FT /note="Contributes to redox potential value"
FT SITE 66
FT /note="Contributes to redox potential value"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:2191628"
FT CONFLICT 41..42
FT /note="DD -> EE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="C -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1DBY"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:1DBY"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1DBY"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1DBY"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:1DBY"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1DBY"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1DBY"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1DBY"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:1DBY"
FT STRAND 109..124
FT /evidence="ECO:0007829|PDB:1DBY"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1DBY"
SQ SEQUENCE 140 AA; 15102 MW; B9CB842F91D872CA CRC64;
MALVARRAAV PSARSSARPA FARAAPRRSV VVRAEAGAVN DDTFKNVVLE SSVPVLVDFW
APWCGPCRII APVVDEIAGE YKDKLKCVKL NTDESPNVAS EYGIRSIPTI MVFKGGKKCE
TIIGAVPKAT IVQTVEKYLN
