ID A0A7R6PFH7_9GAMM Unreviewed; 743 AA. AC A0A7R6PFH7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 14-DEC-2022, entry version 5. 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 ECO:0000313|EMBL:BBB23360.1}; GN ORFNames=CVPH_1541 {ECO:0000313|EMBL:BBB23360.1}; OS Abyssogena phaseoliformis symbiont OG214. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1235283 {ECO:0000313|EMBL:BBB23360.1, ECO:0000313|Proteomes:UP000595698}; RN [1] {ECO:0000313|EMBL:BBB23360.1, ECO:0000313|Proteomes:UP000595698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OG214 {ECO:0000313|EMBL:BBB23360.1}; RA Takaki Y., Shimamura S., Nagai Y., Tsuda M., Yoshida T., Maruyama T.; RT "Genome analysis of deep-sea clam Calyptogena phaseoliformis RT endosymbiont."; RL Submitted (DEC-2012) 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 --------------------------------------------------------------------------- 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; AP012977; BBB23360.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7R6PFH7; -. DR KEGG; aphf:CVPH_1541; -. DR Proteomes; UP000595698; 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; 2.60.40.1250; -; 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; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 2. DR Pfam; PF11412; DsbC; 2. DR Pfam; PF02683; DsbD; 1. DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 2. DR SUPFAM; SSF52833; Thioredoxin-like; 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..20 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT CHAIN 21..743 FT /note="Thiol:disulfide interchange protein DsbD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT /id="PRO_5033183281" FT TRANSMEM 326..358 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 370..394 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 406..426 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 447..480 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 486..510 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 522..543 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 549..567 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 579..598 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DOMAIN 608..743 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DISULFID 118..124 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DISULFID 345..467 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DISULFID 658..661 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" SQ SEQUENCE 743 AA; 81337 MW; F18589B776C9727D CRC64; MKRLLLPLFL LLSAFSLVQV EDDLLPVDKA FVFKASVVNN EILLNWDIAK GYYLYKEKIK ISADFSAQLG NAKFPTAKIR NDEFFGKIGV YRDNAVVVVP VLKGDTESIL LTVSYQGCAD LGVCYPPITK SVALSIGSMR STSLTDNVFN LFSRVTNKAQ SIVEKIIPIS DEPLPADDAF KFSVVAIDAN TLLVKWTIHQ EYYLYHDKFF FDIKGAKFGD IVFPKGKIKD DEFFGKIEVH KGVLEVKIPL INVSNQPITF IVKYQGCWEG GVCYPPQEKT KDITLLSQVD DSNINTAPEK PQAPSIEQVE LNETDQITAL LQQDNILLVL ASFFGFGLLL SLTPCVFPMI PILSGIIVGQ KGEVSTKKAL IMSIVFVLSM SITYSIAGVL AGYFGENLQV LFQTPWILAI FSLIFVALAF SMFGYYEIQL PANLQGKITK ISNGQEGGHL IGVAIMGFLS ALIVGPCVAP PLAGALIYIG QTGDTLLGGL SLFVMSLGMG APLVAIGAGI SKLPKAGGWM DNIKYVFGIL MLAVAIYLLD RIISPLTSLV LWAMLTTISP IAMGALSTQT STSSPWQRIF KALGLIILGY GILLWILVAR GGGDMFQPLS GWGASSITTE SVHIKFERVK SVNELDQILA KAKSNNQIVM LDFYADWCIS CKELERFVFS NASVVNEMAM ANVIALQADV TENNANDKAL MKRFGLVGPP AILFFNNDIE NRSQRIIGEI NAQDFLSHLN KTK //