ID   TRXH1_ARATH             Reviewed;         114 AA.
AC   P29448;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Thioredoxin H1;
DE            Short=AtTrxh1;
DE   AltName: Full=Thioredoxin 1;
DE            Short=AtTRX1;
GN   Name=TRX1; OrderedLocusNames=At3g51030; ORFNames=F24M12.70;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8108503; DOI=10.1104/pp.102.1.327;
RA   Rivera-Madrid R., Marinho P., Brugidou C., Chartier Y., Meyer Y.;
RT   "Nucleotide sequence of a cDNA clone encoding an Arabidopsis thaliana
RT   thioredoxin h.";
RL   Plant Physiol. 102:327-328(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=16945919; DOI=10.1074/jbc.m605784200;
RA   Hara S., Motohashi K., Arisaka F., Romano P.G., Hosoya-Matsuda N.,
RA   Kikuchi N., Fusada N., Hisabori T.;
RT   "Thioredoxin-h1 reduces and reactivates the oxidized cytosolic malate
RT   dehydrogenase dimer in higher plants.";
RL   J. Biol. Chem. 281:32065-32071(2006).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19825616; DOI=10.1093/mp/ssn076;
RA   Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT   "Comparative genomic study of the thioredoxin family in photosynthetic
RT   organisms with emphasis on Populus trichocarpa.";
RL   Mol. Plant 2:308-322(2009).
RN   [8]
RP   INTERACTION WITH FBA6.
RX   PubMed=21782461; DOI=10.1016/j.plaphy.2011.06.009;
RA   van der Linde K., Gutsche N., Leffers H.M., Lindermayr C., Mueller B.,
RA   Holtgrefe S., Scheibe R.;
RT   "Regulation of plant cytosolic aldolase functions by redox-modifications.";
RL   Plant Physiol. Biochem. 49:946-957(2011).
RN   [9]
RP   STRUCTURE BY NMR, AND DISULFIDE BOND.
RX   PubMed=15987893; DOI=10.1110/ps.051477905;
RA   Peterson F.C., Lytle B.L., Sampath S., Vinarov D., Tyler E., Shahan M.,
RA   Markley J.L., Volkman B.F.;
RT   "Solution structure of thioredoxin h1 from Arabidopsis thaliana.";
RL   Protein Sci. 14:2195-2200(2005).
RN   [10]
RP   INTERACTION WITH MDH1.
RX   PubMed=29194485; DOI=10.1093/jxb/erx396;
RA   Huang J., Niazi A.K., Young D., Rosado L.A., Vertommen D., Bodra N.,
RA   Abdelgawwad M.R., Vignols F., Wei B., Wahni K., Bashandy T., Bariat L.,
RA   Van Breusegem F., Messens J., Reichheld J.P.;
RT   "Self-protection of cytosolic malate dehydrogenase against oxidative stress
RT   in Arabidopsis.";
RL   J. Exp. Bot. 69:3491-3505(2018).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase involved in the redox
CC       regulation of a number of cytosolic enzymes. Activates the cytosolic
CC       malate dehydrogenase (MDH) probably by reducing an interchain disulfide
CC       bond of the inactive MDH homodimer. Possesses insulin disulfide bonds
CC       reducing activity. {ECO:0000269|PubMed:16945919}.
CC   -!- SUBUNIT: Interacts with FBA6 (PubMed:21782461). Interacts with MDH1
CC       (PubMed:29194485). {ECO:0000269|PubMed:21782461,
CC       ECO:0000269|PubMed:29194485}.
CC   -!- INTERACTION:
CC       P29448; Q3E9D5: SAMDC4; NbExp=3; IntAct=EBI-8519814, EBI-25512418;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z14084; CAA78462.1; -; mRNA.
DR   EMBL; U35827; AAC49354.1; -; Genomic_DNA.
DR   EMBL; AL132980; CAB62625.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78739.1; -; Genomic_DNA.
DR   EMBL; AY088687; AAM67008.1; -; mRNA.
DR   PIR; JQ2242; JQ2242.
DR   RefSeq; NP_190672.1; NM_114963.5.
DR   PDB; 1XFL; NMR; -; A=1-114.
DR   PDBsum; 1XFL; -.
DR   AlphaFoldDB; P29448; -.
DR   BMRB; P29448; -.
DR   SMR; P29448; -.
DR   BioGRID; 9585; 1.
DR   IntAct; P29448; 46.
DR   MINT; P29448; -.
DR   STRING; 3702.P29448; -.
DR   PaxDb; 3702-AT3G51030-1; -.
DR   ProteomicsDB; 232420; -.
DR   DNASU; 824267; -.
DR   EnsemblPlants; AT3G51030.1; AT3G51030.1; AT3G51030.
DR   GeneID; 824267; -.
DR   Gramene; AT3G51030.1; AT3G51030.1; AT3G51030.
DR   KEGG; ath:AT3G51030; -.
DR   Araport; AT3G51030; -.
DR   TAIR; AT3G51030; TRX1.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_14_1_1; -.
DR   InParanoid; P29448; -.
DR   OMA; MKEWIKQ; -.
DR   OrthoDB; 1215770at2759; -.
DR   PhylomeDB; P29448; -.
DR   EvolutionaryTrace; P29448; -.
DR   PRO; PR:P29448; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P29448; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:TAIR.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:TAIR.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; THIOREDOXIN; 1.
DR   PANTHER; PTHR10438:SF425; THIOREDOXIN H1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; P29448; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q42403"
FT   CHAIN           2..114
FT                   /note="Thioredoxin H1"
FT                   /id="PRO_0000120046"
FT   DOMAIN          2..114
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            41
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            42
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q42403"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT                   ECO:0000269|PubMed:15987893"
FT   STRAND          9..13
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   HELIX           41..56
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   STRAND          58..66
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   STRAND          81..89
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:1XFL"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:1XFL"
SQ   SEQUENCE   114 AA;  12673 MW;  E090761B2187F1F6 CRC64;
     MASEEGQVIA CHTVETWNEQ LQKANESKTL VVVDFTASWC GPCRFIAPFF ADLAKKLPNV
     LFLKVDTDEL KSVASDWAIQ AMPTFMFLKE GKILDKVVGA KKDELQSTIA KHLA
//