ID E3PWS3_ACESD Unreviewed; 75 AA.
AC E3PWS3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Redox-active disulfide protein 2 {ECO:0000313|EMBL:CBH20888.1};
GN OrderedLocusNames=CLOST_0762 {ECO:0000313|EMBL:CBH20888.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH20888.1, ECO:0000313|Proteomes:UP000007041};
RN [1] {ECO:0000313|Proteomes:UP000007041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000313|Proteomes:UP000007041};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
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 EMBL; FP565809; CBH20888.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PWS3; -.
DR STRING; 1511.CLOST_0762; -.
DR KEGG; cst:CLOST_0762; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_090389_18_2_9; -.
DR OMA; DYGVMIT; -.
DR BioCyc; CSTI499177:GJE9-806-MONOMER; -.
DR Proteomes; UP000007041; Chromosome.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR005243; THIRX-like_proc.
DR NCBIfam; TIGR00412; redox_disulf_2; 1.
DR PANTHER; PTHR36450; THIOREDOXIN; 1.
DR PANTHER; PTHR36450:SF1; THIOREDOXIN; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037031-51};
KW Redox-active center {ECO:0000256|PIRSR:PIRSR037031-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007041}.
FT DOMAIN 1..75
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT DISULFID 10..13
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ SEQUENCE 75 AA; 8160 MW; 3A5EC708EFF16D09 CRC64;
MVIKILGSGC ANCKKLEQSA QQAVKELGLE ATIEKVEDFQ EIMAYGVMKT PALVVDEVVK
SSGRVLSAED VKKYL
//