TRXY1_ARATH
ID TRXY1_ARATH Reviewed; 172 AA.
AC Q6NPF9; Q9SRD7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Thioredoxin Y1, chloroplastic;
DE Short=AtTrxy1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g76760; ORFNames=F28O16.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15531707; DOI=10.1104/pp.104.052233;
RA Collin V., Lamkemeyer P., Miginiac-Maslow M., Hirasawa M., Knaff D.B.,
RA Dietz K.J., Issakidis-Bourguet E.;
RT "Characterization of plastidial thioredoxins from Arabidopsis belonging to
RT the new y-type.";
RL Plant Physiol. 136:4088-4095(2004).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19259774; DOI=10.1007/s11103-009-9471-4;
RA Cain P., Hall M., Schroder W.P., Kieselbach T., Robinson C.;
RT "A novel extended family of stromal thioredoxins.";
RL Plant Mol. Biol. 70:273-281(2009).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that poorly activates
CC chloroplastic malate dehydrogenase (NADP-MDH) and fructose-1,6-
CC bisphosphatase. Provides reducing equivalents for peroxiredoxin Q.
CC {ECO:0000269|PubMed:15531707}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15531707, ECO:0000269|PubMed:19259774}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and seeds.
CC {ECO:0000269|PubMed:15531707}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in developing seeds and
CC decreases during seed germination. {ECO:0000269|PubMed:15531707}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant Y-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF04439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010718; AAF04439.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35886.1; -; Genomic_DNA.
DR EMBL; BT010677; AAR20734.1; -; mRNA.
DR EMBL; BT010965; AAR24743.1; -; mRNA.
DR EMBL; AK227422; BAE99426.1; -; mRNA.
DR PIR; B96796; B96796.
DR RefSeq; NP_177802.2; NM_106326.8.
DR PDB; 7BZK; X-ray; 1.59 A; B=63-172.
DR PDBsum; 7BZK; -.
DR AlphaFoldDB; Q6NPF9; -.
DR SMR; Q6NPF9; -.
DR BioGRID; 29229; 13.
DR IntAct; Q6NPF9; 14.
DR STRING; 3702.AT1G76760.1; -.
DR PaxDb; Q6NPF9; -.
DR PRIDE; Q6NPF9; -.
DR ProteomicsDB; 232473; -.
DR EnsemblPlants; AT1G76760.1; AT1G76760.1; AT1G76760.
DR GeneID; 844010; -.
DR Gramene; AT1G76760.1; AT1G76760.1; AT1G76760.
DR KEGG; ath:AT1G76760; -.
DR Araport; AT1G76760; -.
DR TAIR; locus:2030051; AT1G76760.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_3_1; -.
DR InParanoid; Q6NPF9; -.
DR OMA; QTFDSFE; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q6NPF9; -.
DR PRO; PR:Q6NPF9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NPF9; baseline and differential.
DR Genevisible; Q6NPF9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
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 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; Disulfide bond; Electron transport; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..172
FT /note="Thioredoxin Y1, chloroplastic"
FT /id="PRO_0000394539"
FT DOMAIN 63..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 87
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 94
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 95
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 93..96
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:7BZK"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:7BZK"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:7BZK"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:7BZK"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:7BZK"
SQ SEQUENCE 172 AA; 19250 MW; BD1F70B3838BB7DD CRC64;
MASISLSSST VPSLNSKESS GVSAFASRSI SAVKFQFPVR RVRTGDLKFP SLSSTTRCTP
RRIEAKKQTF DSFEDLLVNS DKPVLVDYYA TWCGPCQFMV PILNEVSETL KDKIQVVKID
TEKYPSIANK YKIEALPTFI LFKDGEPCDR FEGALTAKQL IQRIEDSLKV KP
