ID A0A127FBM7_STEDE Unreviewed; 798 AA.
AC A0A127FBM7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ACG33_12090 {ECO:0000313|EMBL:AMN47824.1};
OS Steroidobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN47824.1, ECO:0000313|Proteomes:UP000070250};
RN [1] {ECO:0000313|EMBL:AMN47824.1, ECO:0000313|Proteomes:UP000070250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN47824.1,
RC ECO:0000313|Proteomes:UP000070250};
RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT as an Example.";
RL Submitted (JUN-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
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DR EMBL; CP011971; AMN47824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127FBM7; -.
DR STRING; 465721.ACG33_12090; -.
DR KEGG; sdf:ACG33_12090; -.
DR PATRIC; fig|465721.4.peg.2583; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000070250; Chromosome.
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; 2.
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; 2.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000070250};
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..40
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT CHAIN 41..798
FT /note="Thiol:disulfide interchange protein DsbD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT /id="PRO_5008999114"
FT TRANSMEM 382..412
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 424..449
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 504..534
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 546..569
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 581..599
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 605..622
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 634..653
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DOMAIN 660..797
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 296..302
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 712..715
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ SEQUENCE 798 AA; 84312 MW; 46A6311500C14A6D CRC64;
MILNPLSRSL TRSLTRSLSQ GLSCLLLYLA AMALLPPASA AEDFLQPEQA YRYAGRVDDG
QLILTWTIEP GYYLYKSRMG IAATTPGAVL GEPRWPPGES HTDEFFGTQE IYRGTIEVPV
ALSFASTPPA MLELELKLQG CADAGLCYPP LKWKSTLDLD LAPRGAGPGT AAVAPPGNLR
AGGARALFGR GPAGADDFLS PDEAFRFDAG IADADTLTLT WIIAAGYYLY RDQIQIESAT
PGILLSALRL PAGQPKHDDS YGDTEVYYGV LEATLPIVRT AGSGETLDLR LRYQGCAEDR
LCYNPVVRTV ALMLPPAVTA GSASIPAAST GALPAGPRSR LEPAMNELTF ASRPSNDTAS
NAAAPAEQDR LASLIREGRL PIVLATFFGL GVLLSLTPCV LPMIPILSGI IVGQGGKVTP
ARGFSLALVY VQGMALTYAA AGAAFVLAFK QAPQAFFQQP WIIVVFAALF VALALAMFGA
YDLQLPGALQ TRLASISNRQ KSGTWIGTFV MGALSALIVT ACVAPAIIAA LSVISQTGLI
ARGAGALYAT GLGMGLPLLI VGASAGSLLP KAGPWMSSIK SLFGVLFLAV AIYLLNPLLP
GGLVLLLWAL LAVTTGFWIL SLKSRDGTAV AAPVRGLGVI MLVYGILLLI GAASGGRDPL
QPLDRLRGVD RSSTARELEF QRIKTLDDLQ RAIRRAGAAG KSVMFDVYAD WCISCKEMEK
YTFTDPGVRA ALAGVVLLQA DVTANDGHDQ ALMQYLGIFG PPTIAFFGVD GVERKNFRLV
GFVPAERFQR HVTSAFSG
//
