ID A0A1F1QB62_9PSED Unreviewed; 592 AA.
AC A0A1F1QB62;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399};
DE EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399};
DE AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE Short=Disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE Flags: Precursor;
GN Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN ORFNames=HMPREF3173_09835 {ECO:0000313|EMBL:OFS73939.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS73939.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS73939.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS73939.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000696, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00001346, ECO:0000256|HAMAP-
CC Rule:MF_00399};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|HAMAP-Rule:MF_00399};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|HAMAP-Rule:MF_00399}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000256|ARBA:ARBA00007241, ECO:0000256|HAMAP-Rule:MF_00399}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFS73939.1}.
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DR EMBL; LWMZ01000038; OFS73939.1; -; Genomic_DNA.
DR RefSeq; WP_070572711.1; NZ_KV793303.1.
DR AlphaFoldDB; A0A1F1QB62; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000179079; Unassembled WGS sequence.
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; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 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; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748,
KW ECO:0000256|HAMAP-Rule:MF_00399};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00399};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00399};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00399};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00399}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT CHAIN 19..592
FT /note="Thiol:disulfide interchange protein DsbD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT /id="PRO_5009729702"
FT TRANSMEM 174..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 249..270
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 291..324
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 370..388
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 394..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 422..441
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DOMAIN 446..588
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 135..141
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 189..311
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 503..506
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ SEQUENCE 592 AA; 62438 MW; B40D4347F1620DE5 CRC64;
MRRLFFLLFL LLASPAFAAG LLDNRPSATL GAASLSNSAD FLPVHEAFKL SLVQADAQTV
KLRFVATDGY YLYRHRFKFR TEPADIALGP ADIPKGEAKH DEFFGDVEVY HGVVDIQLPR
TDPRPFTLLV GYQGCADKGL CYPPETERLS IDGTGGKPET GAGGAEQGWG WQSLLLFFLA
GIGLTFTPCV LPMLPILSGV VLRGQVGGWR GLSLSLAYVL PMAVSFAVLG ALMGMFGASL
NLQARLQSAW VLVPFALFFV LFALAMFGLF EIKLPQALSS RLDSMANRTK GGSLLGAAVL
GVLSSLLVSP CVSAPLAGAL LYISASGDAL GGALKLFALG LGMGAPLLLV ATGGAAWLPK
SGPWLNTVKN AVGVLLLGLA IGLLSRVLPG PATLLLVGLL AAGVALFLGA LEFVVKTPRQ
RLAQLLGLAL LVYALACWYG ALSGQGDPLR PLPPPAVASL DASRASKTDA WQTITTPAAL
DAALADAKAA GKPVLLDWYA DWCISCKVIE HEVLSAPQVR SQLGAFKLLR FDITESNAEQ
RTLLDRYQLF GPPALLFFAA NGSELSADRV IGEINAGEFA AILTRVRGKL GL
//
