TRXH_POPJC
ID TRXH_POPJC Reviewed; 139 AA.
AC P85801;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Thioredoxin H-type;
DE AltName: Full=Trxh4;
OS Populus jackii (Balm of Gilead) (Populus deltoides x Populus balsamifera).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=640484;
RN [1]
RP PROTEIN SEQUENCE OF 2-139, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC STRAIN=cv. Beaupre;
RX PubMed=18552403; DOI=10.1074/jbc.m802093200;
RA Koh C.S., Navrot N., Didierjean C., Rouhier N., Hirasawa M., Knaff D.B.,
RA Wingsle G., Samian R., Jacquot J.-P., Corbier C., Gelhaye E.;
RT "An atypical catalytic mechanism involving three cysteines of
RT thioredoxin.";
RL J. Biol. Chem. 283:23062-23072(2008).
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 (By
CC similarity). {ECO:0000250|UniProtKB:O64394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O64394}.
CC -!- MASS SPECTROMETRY: Mass=15515.375; Mass_error=0.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18552403};
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 3D21; X-ray; 2.15 A; A/B=1-139.
DR PDB; 3D22; X-ray; 1.60 A; A=1-139.
DR PDBsum; 3D21; -.
DR PDBsum; 3D22; -.
DR AlphaFoldDB; P85801; -.
DR SMR; P85801; -.
DR EvolutionaryTrace; P85801; -.
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:18552403"
FT CHAIN 2..139
FT /note="Thioredoxin H-type"
FT /evidence="ECO:0000269|PubMed:18552403"
FT /id="PRO_0000341485"
FT DOMAIN 20..132
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P10599,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3D22"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:3D22"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3D22"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:3D22"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:3D22"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3D22"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:3D22"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3D22"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3D22"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:3D22"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3D22"
SQ SEQUENCE 139 AA; 15647 MW; 19631E2A8A4ADDD4 CRC64;
MGLCLAKRNH DADDDEPHIE LAGGNVHLIT TKERWDQKLS EASRDGKIVL ANFSARWCGP
CKQIAPYYIE LSENYPSLMF LVIDVDELSD FSASWEIKAT PTFFFLRDGQ QVDKLVGANK
PELHKKITAI LDSLPPSDK
