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Database: UniProt
Entry: W0E0G9_MARPU
LinkDB: W0E0G9_MARPU
Original site: W0E0G9_MARPU 
ID   W0E0G9_MARPU            Unreviewed;       760 AA.
AC   W0E0G9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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};
GN   Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN   ORFNames=MARPU_01110 {ECO:0000313|EMBL:AHF02611.1};
OS   Marichromatium purpuratum 984.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF02611.1, ECO:0000313|Proteomes:UP000005275};
RN   [1] {ECO:0000313|EMBL:AHF02611.1, ECO:0000313|Proteomes:UP000005275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=984 {ECO:0000313|EMBL:AHF02611.1,
RC   ECO:0000313|Proteomes:UP000005275};
RG   DOE Joint Genome Institute;
RA   Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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}.
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DR   EMBL; CP007031; AHF02611.1; -; Genomic_DNA.
DR   RefSeq; WP_005221806.1; NZ_CP007031.1.
DR   AlphaFoldDB; W0E0G9; -.
DR   STRING; 765910.MARPU_01110; -.
DR   KEGG; mpur:MARPU_01110; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_2_0_6; -.
DR   OrthoDB; 9811036at2; -.
DR   Proteomes; UP000005275; 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; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 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:UP000005275};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        343..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        386..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        466..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        502..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        536..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        563..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        597..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DOMAIN          616..760
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        130..136
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        362..484
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        674..677
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   760 AA;  79721 MW;  F35EE1EF350B6180 CRC64;
     MSRFGPLSRL LPLLLLLALL LPGLAAQARN DFLLPDQAFQ PSAEAIDADT LKVRWQIAEG
     YYLYAAKFAF TTDTAGITLG EPVLPEPEIK QDEFFGEVGI YRDTVEITLP VTRTAAAPEV
     LTLETTSQGC ADAGLCYPPH RQRVQVRLPA PPTAAPAPAI PLPGLDAGAG ISRALGLDDD
     EILTVDQAFD LQVEVLGPER VRLHWEIAPG TYLYRDLVEV ALDDARLALE QPALPPGEIK
     HDSVLPDGSI GDVAVYHDRL TLDLSLRRAT TEALDTTLVV GYQGCAERGI CYPPQTRAVA
     LALPAGGSVA PLAVAPPPAT PAPSAAPVSE QDRLASTLAN ASLWTSMALF FGLGLLLAFT
     PCVFPMIPIL SGIIAGQGAG ITTRRAFVLS LVYVLAMALT YTVAGVLAGL FGANLQAAFQ
     DPWILGAFAL VFIALALSMF GFYDLQLPAA LQSRLAALSN RQQGGTLAGV AIMGLLSALI
     VGPCVAPPLF GALIYISQTG DALLGGVALF ALSLGMGAPL IVIGTSAGKL LPRAGAWMEA
     VKAVFGVALL AVAISLIERV IPAAVAMLLW GLLLICSAVY LGALSPLDHE SGGWRKLWKG
     LGVALLVYGS LMLIGAAAGG KDTLQPLRGL GIGGGEAAHA AFTRVKTVAD LDRELAAASA
     QGRPVMLDFY ADWCVACKEM ERYTFSDPAV IAELDRFVLL QADVTANDAA DQALMQGRFG
     IPGPPAVLFF GTDGAERTGF RLVGFTPAEA FADHLRRAAP
//
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