TRXH1_ARATH
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 03-AUG-2022, entry version 168.
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.AT3G51030.1; -.
DR PaxDb; P29448; -.
DR PRIDE; P29448; -.
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; locus:2080963; AT3G51030.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; P29448; -.
DR OMA; QVGVAPK; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P29448; -.
DR EvolutionaryTrace; P29448; -.
DR PRO; PR:P29448; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P29448; baseline and differential.
DR Genevisible; P29448; AT.
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 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 PIRSF; PIRSF000077; 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; 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
