ID A0A1Z5JI62_FISSO Unreviewed; 967 AA.
AC A0A1Z5JI62;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=FisN_2Hh549 {ECO:0000313|EMBL:GAX13703.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX13703.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX13703.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX13703.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001346};
CC -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC {ECO:0000256|ARBA:ARBA00025782}.
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:GAX13703.1}.
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DR EMBL; BDSP01000072; GAX13703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5JI62; -.
DR InParanoid; A0A1Z5JI62; -.
DR OrthoDB; 5051at2759; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR PANTHER; PTHR13871:SF96; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GAX13703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406}.
FT DOMAIN 627..789
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 967 AA; 108725 MW; BAEB5C09977C9F76 CRC64;
MNTTTSIDAD FKRRIEGGLK TVQAWEDPQL LADCRATIPW EDLKKDDGPF SDENDSFQHS
SYSIIFFQRL CRYFKSGMTW INQPMCPQCQ TTDHVKFVRT RGPETQTEIQ GKASRVEVCQ
CTSCQNENHI AFPRYNCPRT LLQTRQGRCG EYANLFGLYC RAVGYHTRYI LDMTDHVWIE
VCIPNNHRGQ CDYYYCMGDG CEGVVNEPSM YEAGWGKQLS YILAITPSYV MDVTPRYTRQ
FASHDFLARR RAITSSEDAG QAVIQQISAT LLSKLSSVKQ KQSIQKQCRQ EEELLSSHKR
LTEWTKESNL YHQGRISGAT EWKVARGEAG TSSCADGNSE LKDDKNQQLQ HSTEYSIQTF
LPSLHLTQAY IAILPRPPLA QRTQAIVVSG AACAMGIPNQ LSAVVVDPQT GTILQSKSFV
SLQHLEVFVV NLPATLILVV HGQLLKVKNG DRTNLLNMQH RLPLWKSDHV WDGGIIYVGV
VGQTSANATP WTVCAKISDT IDPFILQWNS TASVPDLKLR IHRSTRPNAV TGRLPDSYLP
LAKQVTATFA QKQAAFELFV SASSTTSPKS GQGTSIVGFC TKPGAPIYLI GAGSYPLQPT
SDEWVTFVLL PAWLVPANDC KNGAAALDPV PVSPSLSYEV PLDVNQFVER LGPQLLVNTN
QPIPTDVALQ RKNPRLIALY FSSHWCGPCR SFTPMLIEFY SVLNEAFPTH GLEIVFVSSD
RDVPSFQHYH ATMPWTAIPF EPALQHLKST LSFQFGVQGI PSLVILDAIS GAVVVDARNS
RGEVQQCCRL GDDAIVKQFQ EWLNLLPSES REILDLLQAS CHDTQVAPTL EDGCHDNAVM
IKYVFHENNM DMLETCLSRR GQPITEEDWE SQWRASSKDD WRIVVKTALQ YVVNARREPW
NPKFRIFHWS NAVADRINGV MYGLEWWCRQ GLEVYSSRDD YVAWIPVHVD LEVLHARWSA
LLEDGTQ
//