ID A0A1H8C6W3_9SPHN Unreviewed; 241 AA.
AC A0A1H8C6W3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:SEM90941.1};
GN ORFNames=SAMN05192583_1485 {ECO:0000313|EMBL:SEM90941.1};
OS Sphingomonas gellani.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEM90941.1, ECO:0000313|Proteomes:UP000199206};
RN [1] {ECO:0000313|Proteomes:UP000199206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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DR EMBL; FOCF01000003; SEM90941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8C6W3; -.
DR STRING; 1166340.SAMN05192583_1485; -.
DR OrthoDB; 8478320at2; -.
DR Proteomes; UP000199206; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02972; DsbA_family; 1.
DR Gene3D; 1.10.40.110; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:SEM90941.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199206}.
FT DOMAIN 51..237
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
SQ SEQUENCE 241 AA; 25258 MW; 07F3F485B27ED5C1 CRC64;
MKAVSLLAAI ALTLAGCSGK GGEGNASAPA GSAAAKAPPA GQSWTDVVSK TEEGYRMGNP
DAPVKLVEYG SRLCPACRGF ATEAYQPLTS QYVSTGKVSF EFREFLIHGA ADVPPALLGR
CVGEAAFFPV MEQQYKDQPG FVEKLTPAFM QSIQTLPPQR AFAAMADQMG LVAWFQQRGL
PEAKARQCLA DGKMVDQLTK QTQDKGADGT VTGTPTLIVN GQKVDGIGWG DVEKALKAAG
A
//