ID A0A250X4Y2_9CHLO Unreviewed; 1130 AA.
AC A0A250X4Y2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN ORFNames=CEUSTIGMA_g5548.t1 {ECO:0000313|EMBL:GAX78106.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX78106.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX78106.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX78106.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX78106.1}.
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DR EMBL; BEGY01000029; GAX78106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250X4Y2; -.
DR STRING; 1157962.A0A250X4Y2; -.
DR OrthoDB; 257613at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003882; Pistil_extensin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF23; PEROXIREDOXIN DOT5; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PRINTS; PR01218; PSTLEXTENSIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1031..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 482..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 118600 MW; 824B82D2BCC1A792 CRC64;
MMQTTVRRQT MTCQPLSSMP VSAKLVTYKP SKPQLRCNLV AYALKAGDML PSFELPTDAS
TPEKMIYANT QDMVKDSGVV IFIYPKAATS GCTTQACGFN DNLDRFIKAG FKVYGMSADT
PAEQAAWKSV HGFNYPLLCD MKFQVLPALT GSEKGILYFK AIRELLKLKA IVRHASPYVR
SYASALCMDA AIIIGYVKEV CLFKSVDFHT LLNQRRLPSL LAKNMSKTHI GHRHKFLRFH
RHEAAVHRSL IIFLAWVICR LLRPAESANP PSLFPPPSPP LTPPPPPGTQ YVNTTICLSQ
TWKQGGTAGY VMFTALGFQL SDFSTPSTVQ FVSWSTLNFT VVDGANTFSF SGDALIGSNG
TSYLYPSATS INSQCTTNLS SGLWTSYDVI NSPGNTFLSS TATTVPSTGY SKDSVATWCG
FIQSPGKTQL TMWSRMFPST CSNLYSSNVV ACEDSRLTAN SGRHFGAPMN CLASAVTGGS
NGGNAPNMNI GATPSPPPVP PSPSPPLPAP PSPPDPSPQP PPSPPPSPPP PSPLPLPPPS
TSPLPFPSPP TLPSPPTPLP PPFPPPSTPP SPPTPSLTEP PSPPPSPPPS PPPSPSPLPP
PASSPSTSSP SPLPPPSPPP SPPLSPFPQI PSPSPPLPPS SPPPSPPPSP TLSPSPKSPS
PPHSPPPSPP PVPPPSLPPL PPPAPSPQRP PSPPSIPPPM PPSSQLPLPF PPHFQPSTPS
LSPMSFPSPP HPPYPLLFSP PFPQNVSFNP PFFSPIKPPQ PLSANPAPPP RPSSIPISVT
PPSPSPSSRI SPPTIGPSPM APPFPLGSVD LIVNVTLSGI SLTDFLNVSS GLQVMYQKTL
ATYILGSAQL YQQVLIFSVT QDNAASGTRR RHALSQQDVG RGHALSQQDL GREQQINVLF
MKDDATKGVN DHGRYDGNVD NKEQRVIQLR STLTIADAGA ATTSSTLSST HISVSSSTIL
TTPSVAESAA SSLQNAYSSG SLTTSLIGAG LPTTVGVVGF SAIQNQASSL SPVPSPSGIV
SSGSSSALST IAIAMICVGV VVVGTAVTVI AVRQRSRMSL QGVERKPVDG VVPPAVSSTV
GSGAPPSGPR AGNMLSRWLG GGSDRSHSHG RREYPTGLDI FAEVKTLEMR
//
