TRXH_CHLRE
ID TRXH_CHLRE Reviewed; 113 AA.
AC P80028;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Thioredoxin H-type;
DE Short=Trx-H;
DE AltName: Full=Thioredoxin-CH1;
GN Name=TRXH;
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 PROTEIN SEQUENCE OF 2-112, AND DISULFIDE BOND.
RC STRAIN=137c / CC-125;
RX PubMed=2040309; DOI=10.1111/j.1432-1033.1991.tb16043.x;
RA Decottignies P., Schmitter J.-M., Dutka S., Jacquot J.-P.,
RA Miginiac-Maslow M.;
RT "Characterization and primary structure of a second thioredoxin from the
RT green alga, Chlamydomonas reinhardtii.";
RL Eur. J. Biochem. 198:505-512(1991).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=9030762; DOI=10.1111/j.1432-1033.1997.0374a.x;
RA Mittard V., Blackledge M.J., Stein M., Jacquot J.-P., Marion D.,
RA Lancelin J.-M.;
RT "NMR solution structure of an oxidised thioredoxin h from the eukaryotic
RT green alga Chlamydomonas reinhardtii.";
RL Eur. J. Biochem. 243:374-383(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11563970; DOI=10.1042/0264-6021:3590065;
RA Menchise V., Corbier C., Didierjean C., Saviano M., Benedetti E.,
RA Jacquot J.-P., Aubry A.;
RT "Crystal structure of the wild-type and D30A mutant thioredoxin h of
RT Chlamydomonas reinhardtii and implications for the catalytic mechanism.";
RL Biochem. J. 359:65-75(2001).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of the active center dithiol to a disulfide. The H
CC form is known to activate a number of cytosolic enzymes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This thioredoxin cannot be used as a substrate for
CC E.coli NADPH: thioredoxin reductase, but is a substrate of spinach
CC ferredoxin-thioredoxin reductase and can activate NADP-MDH.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
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DR EMBL; X78822; CAA55399.1; -; mRNA.
DR EMBL; X80887; CAA56850.1; -; Genomic_DNA.
DR PIR; S57775; S57775.
DR RefSeq; XP_001694574.1; XM_001694522.1.
DR PDB; 1EP7; X-ray; 2.10 A; A/B=2-113.
DR PDB; 1EP8; X-ray; 2.20 A; A/B=2-113.
DR PDB; 1TOF; NMR; -; A=2-113.
DR PDB; 6I19; X-ray; 1.38 A; A/B=1-113.
DR PDB; 6Q46; X-ray; 1.70 A; A/B=1-113.
DR PDB; 6Q47; X-ray; 1.57 A; A/B=1-113.
DR PDB; 6Q6T; X-ray; 0.94 A; A=1-113.
DR PDB; 6Q6U; X-ray; 1.81 A; A/B=1-113.
DR PDB; 6Q6V; X-ray; 1.22 A; A/B=1-113.
DR PDBsum; 1EP7; -.
DR PDBsum; 1EP8; -.
DR PDBsum; 1TOF; -.
DR PDBsum; 6I19; -.
DR PDBsum; 6Q46; -.
DR PDBsum; 6Q47; -.
DR PDBsum; 6Q6T; -.
DR PDBsum; 6Q6U; -.
DR PDBsum; 6Q6V; -.
DR AlphaFoldDB; P80028; -.
DR SMR; P80028; -.
DR STRING; 3055.EDP02569; -.
DR PRIDE; P80028; -.
DR ProMEX; P80028; -.
DR EnsemblPlants; PNW78569; PNW78569; CHLRE_09g391900v5.
DR GeneID; 5720085; -.
DR Gramene; PNW78569; PNW78569; CHLRE_09g391900v5.
DR KEGG; cre:CHLRE_09g391900v5; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_10_2_1; -.
DR OrthoDB; 1482186at2759; -.
DR EvolutionaryTrace; P80028; -.
DR GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Electron transport; Redox-active center; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2040309"
FT CHAIN 2..113
FT /note="Thioredoxin H-type"
FT /id="PRO_0000120055"
FT DOMAIN 2..112
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 37
FT /note="Nucleophile"
FT ACT_SITE 40
FT /note="Nucleophile"
FT SITE 31
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 38
FT /note="Contributes to redox potential value"
FT SITE 39
FT /note="Contributes to redox potential value"
FT DISULFID 37..40
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:2040309"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6Q6T"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6Q6T"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6Q6T"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1TOF"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:6Q6T"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6Q6T"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6Q6T"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6Q6T"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:6Q6T"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:6Q6T"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:6Q6T"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6Q6T"
SQ SEQUENCE 113 AA; 11844 MW; BCDDDCFA7810D3EE CRC64;
MGGSVIVIDS KAAWDAQLAK GKEEHKPIVV DFTATWCGPC KMIAPLFETL SNDYAGKVIF
LKVDVDAVAA VAEAAGITAM PTFHVYKDGV KADDLVGASQ DKLKALVAKH AAA
