ID   DSBD_IDILO              Reviewed;         568 AA.
AC   Q5QVU3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399};
DE            EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399};
DE   AltName: Full=Protein-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE            Short=Disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE   Flags: Precursor;
GN   Name=dsbD {ECO:0000255|HAMAP-Rule:MF_00399}; OrderedLocusNames=IL2283;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- FUNCTION: Required to facilitate the formation of correct disulfide
CC       bonds in some periplasmic proteins and for the assembly of the
CC       periplasmic c-type cytochromes. Acts by transferring electrons from
CC       cytoplasmic thioredoxin to the periplasm. This transfer involves a
CC       cascade of disulfide bond formation and reduction steps.
CC       {ECO:0000255|HAMAP-Rule:MF_00399}.
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:0000255|HAMAP-Rule:MF_00399};
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:0000255|HAMAP-Rule:MF_00399};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00399}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00399}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00399}.
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DR   EMBL; AE017340; AAV83115.1; -; Genomic_DNA.
DR   RefSeq; WP_011235509.1; NC_006512.1.
DR   AlphaFoldDB; Q5QVU3; -.
DR   SMR; Q5QVU3; -.
DR   STRING; 283942.IL2283; -.
DR   EnsemblBacteria; AAV83115; AAV83115; IL2283.
DR   KEGG; ilo:IL2283; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_3_0_6; -.
DR   OMA; YRHRFQF; -.
DR   OrthoDB; 1055204at2; -.
DR   Proteomes; UP000001171; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR   CDD; cd02953; DsbDgamma; 1.
DR   Gene3D; 2.60.40.1250; -; 1.
DR   HAMAP; MF_00399; DbsD; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036929; DsbDN_sf.
DR   InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR   Pfam; PF11412; DsbC; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF74863; SSF74863; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   CHAIN           23..568
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000304390"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DOMAIN          416..567
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        128..134
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        190..311
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT   DISULFID        482..485
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   568 AA;  62859 MW;  7D26ABB10295C0C4 CRC64;
     MIQRFITCLA ALTLVFAVVA PAHSVQSNPF QQDNQFLSVD QAFDFDSEVN DSKVTVSWVV
     APEYYLYQHR FKVVPENALA AEPELPQGES HNDEFFGESI VYRNYVEWSF TLNPEFSGDT
     ITVQYQGCAD AGLCYPPTEK QIKLSSTSET APATAPPNTD SSLFGIGEQH LIITLLLFFA
     LGIGLAFTPC VFPMYPILSG VVLGNRERNW KNTLWLSFIY VQGMAITYSL LGLVVASAGM
     QYQAYFQHPV VLIVLAVLFA LFALSMFGAY TLQLPISWQS KLQSFSGQQS GGNIVGVFII
     GAISGLVASP CTTAPLSGAL LFIAQSGDMV SGVAILYALS LGMGVPLILF GLSGGKLLPK
     AGAWMNVVKQ FFGWLLLAVT LFLIERLIPT SISMWLWIFY FILAAVSLAV SISQPLRITT
     KVITIVLLAA AATTGSYWQV NKAQLEQKSH GLFTVVSNVS DIQQQVAESD RWVMLDLYAD
     WCVACKEFEQ YTFSDEQVQA QFQEFKLIQA DVTRNNAQDV EILSRYKVLG LPTILFFDPE
     GNERPEYRVT GYMNAEDFKK HLEKIVSE