ID Q46WH2_CUPPJ Unreviewed; 639 AA. AC Q46WH2; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 124. 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 OrderedLocusNames=Reut_A3151 {ECO:0000313|EMBL:AAZ62511.1}; OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator OS (strain JMP 134)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ62511.1}; RN [1] {ECO:0000313|EMBL:AAZ62511.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JMP134 {ECO:0000313|EMBL:AAZ62511.1}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., RA Larimer F., Land M., Lykidis A., Richardson P.; RT "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134."; RL Submitted (AUG-2005) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000090; AAZ62511.1; -; Genomic_DNA. DR AlphaFoldDB; Q46WH2; -. DR STRING; 264198.Reut_A3151; -. DR KEGG; reu:Reut_A3151; -. DR eggNOG; COG4232; Bacteria. DR HOGENOM; CLU_014657_3_0_4; -. DR OrthoDB; 9811036at2; -. 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; 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; 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; 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}; 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..39 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT CHAIN 40..639 FT /note="Thiol:disulfide interchange protein DsbD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT /id="PRO_5009019185" FT TRANSMEM 212..233 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 254..278 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 331..364 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 376..399 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 411..428 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 434..455 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 467..487 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DOMAIN 488..634 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DISULFID 143..149 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DISULFID 550..553 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" SQ SEQUENCE 639 AA; 67140 MW; 6F99003AB556A031 CRC64; MSMGFALLAR SYGAGWARHI AAVLAVMVAW LCLVTGAHAA TEDDFLPPEQ AFRFAARQID PQTIEVRFDV ASGYYLYRER FAFAARPDTV RLGQPEFPHG KVKFDETFGK EMETYRDAVV IRLPVQSAPA DGKWSLVVTS QGCADKGLCY PPMESVYKVG GSPLGNLFAD RPRSEATVPP AASARPGTEA VAPPARLDEN DRIAGVLASR NLGVVLALFF GLGLLLTFTP CVLPMVPILS SIVVGEHATR SRALVVSLAY VLGMAVVYTA IGVAAGLLGE GLAAALQTPA VLAAFAALMV ALSLSMFGLY ELQLPQHWQT RLTATSNRRQ GGQVIGAAAM GAISALIVGP CVTAPLAGAL AYIAQTRDAV TGGTALLAMA LGMGVPLVLV GVGAGNLLPR AGHWMEATKR FFGFLLLGVA IWMVTPVLPA WLTMALWAAL LLVAAVFLGA FDALGAEARG LARLGKGLGV LAALAGAILL LGLASGGRDP LQPLAHLSLA RVAGGGAETA AGPQSVRFER VRSVAELDAR VAQAAAAGKP VLLDFYADWC VSCKEMEHLT FTDAKVRARM SEIVLLQADV TANNADDKAL LKRFGLFGPP GIILFGADGR ERPVRVIGYQ SAGRFLDSLE RAFGTRPST //