ID A0A011QGU7_ACCRE Unreviewed; 608 AA. AC A0A011QGU7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JAN-2024, entry version 38. 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 ECO:0000313|EMBL:EXI88517.1}; GN ORFNames=AW11_02137 {ECO:0000313|EMBL:EXI88517.1}; OS Accumulibacter regalis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter. OX NCBI_TaxID=522306 {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141}; RN [1] {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EXI88517.1}. 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; JEMY01000026; EXI88517.1; -; Genomic_DNA. DR AlphaFoldDB; A0A011QGU7; -. DR STRING; 1454004.AW11_02137; -. DR PATRIC; fig|1454004.3.peg.2214; -. DR eggNOG; COG4232; Bacteria. DR Proteomes; UP000022141; Unassembled WGS sequence. 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}; Reference proteome {ECO:0000313|Proteomes:UP000022141}; 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 191..218 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 238..261 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 273..296 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 317..347 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 359..383 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 395..412 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT TRANSMEM 448..469 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DOMAIN 467..608 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DISULFID 138..144 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" FT DISULFID 524..527 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399" SQ SEQUENCE 608 AA; 64989 MW; 497E8D24EF2DC87E CRC64; MTWLFVLPHS VRRFFQRSSL LPFLLPVLML LTWPAQGEEF LDPAVAFKPT AHAVDGQTIE VRFEIAKGYY LYRDKFRFTA EPASVQLGTP ILSPGKVKED PNFGKVEVYY KQALIRIPVE RNSSGPLPLT LKITSQGCAD AGICYPPQRQ TLALELPDPA TTPSAGATTP GKDFGDDESG RIAQLFGNAS FWLLVASFFG FGLLLSLTPC CFPMIPILSS IIVGSGRDGH GVSHARGFSL SLAYVLGMAI TYAAAGVAAG LTGTLLTAAL QNAWVLGAFA LVFVALSLSM FGFYELQLPT FLQSKVSEEA SHLRGGSLPG VAAMGVLSAI IVGPCVAAPL AGALLYIGRS GDAVLGGAAL FAMGLGMGAP LLAVGLSAGT LLPRSGPWME AVKKSFGVLL LATAVWLLSP VVPVVAQMIA WALLLIVPAI YMHALDPLPP HARGWQRFWK GIGIFMLIGG AAMLLGALAG SRDPLQPLSA LRSSAAEVEV KQLPFTRVRT LAELERRIKS AGQPVMIDFY ADWCVSCKEM ERFTFADARV RAKLAGWTLL QADVTANSDE DKALLQRFNL YGPPGIIFFD AQGREIDGVR VVGFMSADEF LGLLARLG //