ID H8L372_FRAAD Unreviewed; 418 AA.
AC H8L372;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Thiol-disulfide isomerase-like thioredoxin {ECO:0000313|EMBL:AFC85508.1};
GN OrderedLocusNames=Fraau_1047 {ECO:0000313|EMBL:AFC85508.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC85508.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003350; AFC85508.1; -; Genomic_DNA.
DR RefSeq; WP_014402514.1; NC_017033.1.
DR AlphaFoldDB; H8L372; -.
DR STRING; 767434.Fraau_1047; -.
DR KEGG; fau:Fraau_1047; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_675960_0_0_6; -.
DR OrthoDB; 9798454at2; -.
DR Proteomes; UP000005234; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:AFC85508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005234};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003614870"
FT DOMAIN 254..414
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 418 AA; 45951 MW; 5BEB62D76A195AE3 CRC64;
MMFLRALLLG LSLPTAVMAG DAGLKPWLGD WQATASQSSQ NIPFHYQIVQ DGQRQLHGNF
FNGSDAITSQ PATPRNGHLI LRYPGFDRVL DLQLRTDGSL DGRYTAIQSG PHSPSWTIKA
RRPAASTASS GVAPDIDGLW LVPAASRKHN EHAWRLIVRQ QFSEVSAAVL GVGGDTGALT
GTWHDGSWQL SNFSGTRAET ASLKPDHAAN GDVDLQLDLT DSHGQHSHYL AYRPETARKL
GLPEAADLGN HTTVRDPDEI FAFSFPDLQG HRISNTDARF RHKVVLLDVS GSWCPNCHDE
APFLEALYRR YHARGLEIVT LDFEDKDQFK DPARLRAFIA ESHTSFPVLL AGTTDQAQEK
LPQAVNLDAW PTTFFIARDG RVKHIHTGFS AKATGVYHSA LTREFEQQIE TLLAAPAG
//