ID DSBD_HAEDU Reviewed; 573 AA. AC Q7VMZ4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 02-SEP-2026, entry version 134. DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399}; DE EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399}; DE AltName: Full=Protein-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399}; DE Short=Disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399}; DE Flags: Precursor; GN Name=dsbD {ECO:0000255|HAMAP-Rule:MF_00399}; GN OrderedLocusNames=HD_0807; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., RA Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) 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:0000255|HAMAP-Rule:MF_00399}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + NADH + CC H(+); 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:0000255|HAMAP-Rule:MF_00399}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + NADPH + CC H(+); 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:0000255|HAMAP-Rule:MF_00399}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00399}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000255|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; AE017143; AAP95707.1; -; Genomic_DNA. DR RefSeq; WP_010944757.1; NC_002940.2. DR AlphaFoldDB; Q7VMZ4; -. DR SMR; Q7VMZ4; -. DR STRING; 233412.HD_0807; -. DR KEGG; hdu:HD_0807; -. DR eggNOG; COG4232; Bacteria. DR HOGENOM; CLU_014657_3_0_6; -. DR OrthoDB; 9811036at2; -. DR Proteomes; UP000001022; 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)H] activity; IEA:UniProtKB-UniRule. DR GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule. DR CDD; cd02953; DsbDgamma; 1. DR FunFam; 3.40.30.10:FF:000116; Thiol:disulfide interchange protein DsbD; 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; IPR061926; DsbD_link. DR InterPro; IPR028250; DsbDN. DR InterPro; IPR036929; DsbDN_sf. DR InterPro; IPR022910; Thiol_diS_interchange_DbsD. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; NF001419; PRK00293.1; 1. DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1. DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1. DR Pfam; PF30370; DsbD_link; 1. DR Pfam; PF11412; DsbD_N; 1. DR Pfam; PF02683; DsbD_TM; 1. DR Pfam; PF13098; Thioredoxin_2; 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; Cell membrane; Cytochrome c-type biogenesis; KW Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase; KW Redox-active center; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1..20 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT CHAIN 21..573 FT /note="Thiol:disulfide interchange protein DsbD" FT /id="PRO_0000007375" FT TOPO_DOM 21..175 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 197..227 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 228..248 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 249..251 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 252..272 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 273..292 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 293..313 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 314..331 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 332..352 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 353..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 387..393 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 394..414 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 415..425 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 426..446 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TOPO_DOM 447..573 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT DOMAIN 440..573 FT /note="Thioredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DISULFID 121..126 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DISULFID 191..313 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DISULFID 490..493 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" SQ SEQUENCE 573 AA; 63070 MW; 2D1D3A9C7E3632D6 CRC64; MLKRFFLLLS SLLLVCNVQA GLFNNKPQYL TAAEAFIFSS SQQDGQLQLH WQIADGYYLY QKEIQLSAQN ATLGDVTFPT AEKYQDEFFG EVAIFRDQLK LPVKLTDLKE NPSLKIRYQG CTKGFCYPPE TVVIPLNPSL QGNNSANSAA LPSTIATPNA PQTELAENLS NNYLSIFGFL LLGIGLAFTP CVLPMLPLLS AIVIGHKNRP NTSRALLLSF TYVQGMALTY TLLGLTVAAI GLPFQVALQS PAVLISLAVL FTLLAASMFG LFEIRLPNTW QQKLNALSQQ QQGGAVGNVF IMGIIAGLVA SPCTSAPLSG ALLYVAQSGN LLIGGLALYL LALGMGLPLI LITVFGNQIL PKSGEWLFKV KTAFGFVMLA LPIFLISRIL PSHYEPFLWS TLALAFLGWL ISSLNYSTML KQAVRILLFI AFGLTAYPWA NLVWQTTSNT AQPTTPHLAM EKITSLTELE QKLTAYQGKK VMLDLYADWC VACKEFEKYT FTDPQVQQQL ATMAVLQIDM TKNSAENTAL MKHFNVLGLP TILFFDENGH EMTNVRITGF LTANQFLAWL NRL //