ID DSBD_PHOLL Reviewed; 575 AA. AC Q7MZX2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 04-NOV-2026, entry version 153. 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=plu4139; OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / OS TT01) (Photorhabdus luminescens subsp. laumondii). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., RA Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). 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; BX571872; CAE16511.1; -; Genomic_DNA. DR RefSeq; WP_011148255.1; NC_005126.1. DR AlphaFoldDB; Q7MZX2; -. DR SMR; Q7MZX2; -. DR STRING; 243265.plu4139; -. DR GeneID; 48850356; -. DR KEGG; plu:plu4139; -. DR eggNOG; COG4232; Bacteria. DR HOGENOM; CLU_014657_3_0_6; -. DR OMA; AACYEFE; -. DR OrthoDB; 9811036at2; -. DR Proteomes; UP000002514; 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; dsbD; 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..24 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT CHAIN 25..575 FT /note="Thiol:disulfide interchange protein DsbD" FT /id="PRO_0000304391" FT TRANSMEM 180..200 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 216..236 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 253..273 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 297..317 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 367..387 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 394..414 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT TRANSMEM 425..445 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DOMAIN 444..575 FT /note="Thioredoxin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DISULFID 126..132 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399" FT DISULFID 192..314 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 575 AA; 64073 MW; CBEC7F62BF5E7852 CRC64; MIKRTLMLFL LLCSPLLTPA AANALFEQPG QNPYLPVDQA FMFDFQQKGD KLTLDWQIKP GYYLYHKQLH IEPQQATLGK ITLPQGTAHR DEFFGETEVY FQQLIVNVPV TKANNNSNIV VTYQGCAAAG YCYPPETRLV PLSAVIPSKT TDAISAEPVH KTPESASNDQ QHLPFSPLWA ILIGIGIAFT PCVLPMYPLI SSIILGSQRP KSLKQIFWLA LSYVQGMAVT YTLLGLIVAA AGLQFQAALQ HPYVLIGLSV LFILLALSMF GLYSLQLPSA VQTRLVNWSN QQKNGSLFGV FAMGALAGLI CSPCTTAPLS AILLYIAQSG NTVAGGLTLY LYALGMGLPL IAVTLFGHKL LPRSGPWMQY VKEAFGFIIL ALPVFLLERV IGDAWGIRLW SLLAVSFLGW GFVLTIRSQN GWVRVIQLIL LILMLIATRP LQDWFWGTTV TQQSQHSLNF RQINNWQELE QIMTQNSHKT VMLDFYADWC TACKEFEKYT FSDPQVQSQL GDTLLLQANV TNNSPQQKQL LEKLSVRGLP TILFFDSQGK EIPDSRVNGF MDATRFNEHL QHLPK //