TRXM1_ARATH
ID TRXM1_ARATH Reviewed; 179 AA.
AC O48737;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Thioredoxin M1, chloroplastic;
DE Short=AtTrxm1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g03680; ORFNames=F21B7.28, F21B7_7;
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=10580150; DOI=10.1016/s0378-1119(99)00448-5;
RA Mestres-Ortega D., Meyer Y.;
RT "The Arabidopsis thaliana genome encodes at least four thioredoxins m and a
RT new prokaryotic-like thioredoxin.";
RL Gene 240:307-316(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION.
RX PubMed=19631646; DOI=10.1016/j.febslet.2009.07.035;
RA Nee G., Zaffagnini M., Trost P., Issakidis-Bourguet E.;
RT "Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new
RT role for f-type thioredoxin.";
RL FEBS Lett. 583:2827-2832(2009).
RN [6]
RP FUNCTION.
RX PubMed=19825612; DOI=10.1093/mp/ssn061;
RA Marri L., Zaffagnini M., Collin V., Issakidis-Bourguet E., Lemaire S.D.,
RA Pupillo P., Sparla F., Miginiac-Maslow M., Trost P.;
RT "Prompt and easy activation by specific thioredoxins of calvin cycle
RT enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK
RT supramolecular complex.";
RL Mol. Plant 2:259-269(2009).
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 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 involved in the redox
CC regulation of enzymes of both reductive pentose phosphate pathway
CC (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under
CC reducing conditions, activates the glyceraldehyde-3-phosphate
CC dehydrogenase and the phosphoribulokinase, and inhibits. the glucose-6-
CC phosphate dehydrogenase. Activates NADP-malate dehydrogenase.
CC {ECO:0000269|PubMed:19631646, ECO:0000269|PubMed:19825612}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19259774}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF095749; AAF15948.1; -; mRNA.
DR EMBL; AC002560; AAF86525.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27596.1; -; Genomic_DNA.
DR EMBL; BT004295; AAO42293.1; -; mRNA.
DR EMBL; BT005525; AAO63945.1; -; mRNA.
DR PIR; T00893; T00893.
DR RefSeq; NP_849585.1; NM_179254.7.
DR PDB; 7C65; X-ray; 1.10 A; A=71-179.
DR PDBsum; 7C65; -.
DR AlphaFoldDB; O48737; -.
DR SMR; O48737; -.
DR BioGRID; 24671; 3.
DR IntAct; O48737; 1.
DR STRING; 3702.AT1G03680.1; -.
DR MetOSite; O48737; -.
DR PaxDb; O48737; -.
DR PRIDE; O48737; -.
DR ProteomicsDB; 232395; -.
DR EnsemblPlants; AT1G03680.1; AT1G03680.1; AT1G03680.
DR GeneID; 839436; -.
DR Gramene; AT1G03680.1; AT1G03680.1; AT1G03680.
DR KEGG; ath:AT1G03680; -.
DR Araport; AT1G03680; -.
DR TAIR; locus:2020813; AT1G03680.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_2_1; -.
DR InParanoid; O48737; -.
DR OMA; LITCIER; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; O48737; -.
DR PRO; PR:O48737; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48737; baseline and differential.
DR Genevisible; O48737; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor 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; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
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..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..179
FT /note="Thioredoxin M1, chloroplastic"
FT /id="PRO_0000034162"
FT DOMAIN 67..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 98
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 105
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 106
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 104..107
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:7C65"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7C65"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:7C65"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:7C65"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:7C65"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:7C65"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:7C65"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7C65"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:7C65"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:7C65"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:7C65"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:7C65"
SQ SEQUENCE 179 AA; 19665 MW; 35B9E7C1D132F492 CRC64;
MAAYTCTSRP PISIRSEMRI ASSPTGSFST RQMFSVLPES SGLRTRVSLS SLSKNSRVSR
LRRGVICEAQ DTATGIPVVN DSTWDSLVLK ADEPVFVDFW APWCGPCKMI DPIVNELAQK
YAGQFKFYKL NTDESPATPG QYGVRSIPTI MIFVNGEKKD TIIGAVSKDT LATSINKFL
