DSBD_PSEUK
ID DSBD_PSEUK Reviewed; 578 AA.
AC Q9KJZ3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Thiol:disulfide interchange protein DsbD;
DE EC=1.8.1.8;
DE AltName: Full=Protein-disulfide reductase;
DE Short=Disulfide reductase;
DE Flags: Precursor;
GN Name=dsbD;
OS Pseudomonas sp. (strain JR1 / K1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=269087;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Johann A., Michel J., Averhoff B., Gottschalk G.;
RT "The two-component signal transduction system ArmRS is involved in
RT deregulation of 3-isopropylcatechol dioxygenase in the mutant strain
RT Pseudomonas sp. K1.";
RL Submitted (JUN-1999) 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 (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000305}.
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DR EMBL; AF155506; AAF80267.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KJZ3; -.
DR SMR; Q9KJZ3; -.
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; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..578
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007383"
FT TOPO_DOM 19..158
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..237
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..321
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..578
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 433..576
FT /note="Thioredoxin"
FT DISULFID 118..124
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 179..299
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 491..494
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 62181 MW; 7473FC17A9BF7284 CRC64;
MRRLFLFFAL LISGVAQAGT NPFETKPDFL PVGKAFVFTS ERLESGETQL YWQIADGYYL
YQKRLKFDGL PAEQHPALPE GETHSDEFFG EQQVYRQGLE LKIAAGATGQ IKVGFQGCAD
AGLCYPPHTQ VVDLGGYLRY RCDRRSTGPS PGQRLQQRAL GWSLLVFFGL GLLLAFTPCS
LPMLPILAGL IVGSGATPKR GFALATSYVV SMALVYAAMG VLAAMLGANL QALLQNPWLL
GSFAAVFVLL ALPMFGFFEL QLPVAVRDRL ENVSRNQRGG SLFGAGVLGA LSGLLVGPCM
TAPLAGALLY IAQSGNALHG GLILFAMGIG IGVPLLLLVT VGNRFLPKPG AWMNLLKGVF
GFLFLATALL MLRPVLDESL WIGLCGGLLL IAAYSAWKQS EGFGRVAHVF GASSLLLGVW
GSLLMIGAAG GSDDLMKPLQ VYSASNSSSA ANPVSHDAFT TIKDPAALQR ELDEAQAQGQ
WVLLDYYADW CVSCKVMEKQ VFGKAHVMEA LSDVRLLRLD VTADNAASRE LLGRYKVPGP
PSLLWIGADG IERRSQRITG EVDAGTFLQR WTTTRDAH
