ID E1QGV8_DESB2 Unreviewed; 480 AA.
AC E1QGV8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ADK84801.1};
GN OrderedLocusNames=Deba_1433 {ECO:0000313|EMBL:ADK84801.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84801.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK84801.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
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DR EMBL; CP002085; ADK84801.1; -; Genomic_DNA.
DR AlphaFoldDB; E1QGV8; -.
DR STRING; 644282.Deba_1433; -.
DR KEGG; dbr:Deba_1433; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_568292_0_0_7; -.
DR OrthoDB; 9813820at2; -.
DR Proteomes; UP000009047; Chromosome.
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; IPR013740; Redoxin.
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; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..480
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003150348"
FT DOMAIN 15..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 456..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 51792 MW; BB9275B5E82BBCD5 CRC64;
MKTPRIWLAA ALIALCALGA QPSWSMDFNR PTLEGQALSL SQFRGRVVLL DFFATWCGPC
TQAMPKLRQL QSAYGHAGLS IVGYSVDSGG LEAVGPYAAR NRLNFPVVLG NAAEAKRIAG
VTALPTTVII DPEGRVAARF EGPVSKERLI GVIKPYLREG AAPAPPAAKV ELRANGANRF
NRVWVTPNML FQGQLGLFVH TVVDVSDLYT KQGLWLGITM TPETIAPDGS TRPQGPPVTK
YQRVDEAWRK HFILFLTCGQ MPPMTGRGAY RSQIFLLGPG QKVIERSEDF WISDECQTGA
AGSPSQFEEA KMDFGGGGPR KTGMVGKWRW AGQDRLRGAW LTGPTVHQGR SGLFVHVEAD
FSQDDLKRGL ALGLDFAGAA QGRSATPRAE SRLVQLVEAD NPGYYIMFIG CDQLPAQVAG
GDGAMWVSLL AGPERQELER SGVFIIDEAI CDGRAASQTS GGRQRRSGMA PGDDSPWGGF
//
