ID A0A011QGU7_9PROT Unreviewed; 608 AA. AC A0A011QGU7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 13-NOV-2019, entry version 26. 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 Candidatus Accumulibacter sp. BA-93. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter; unclassified Candidatus Accumulibacter. OX NCBI_TaxID=1454004 {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 CC disulfide bonds in some periplasmic proteins and for the assembly CC of the periplasmic c-type cytochromes. Acts by transferring CC electrons from cytoplasmic thioredoxin to the periplasm. This CC transfer involves a cascade of disulfide bond formation and CC reduction steps. {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, CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.8.1.8; Evidence={ECO:0000256|HAMAP-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, CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.8.1.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00399}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00399}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 STRING; 1454004.AW11_02137; -. DR PATRIC; fig|1454004.3.peg.2214; -. DR Proteomes; UP000022141; Unassembled WGS sequence. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 activity; IEA:UniProtKB-UniRule. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule. DR CDD; cd02953; DsbDgamma; 1. DR Gene3D; 2.60.40.1250; -; 1. DR Gene3D; 3.40.30.10; -; 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:SF0; PTHR32234:SF0; 1. DR Pfam; PF11412; DsbC; 1. DR Pfam; PF02683; DsbD; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF74863; SSF74863; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00399}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399}; KW Complete proteome {ECO:0000313|Proteomes:UP000022141}; KW Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00399}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464083}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00399}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000313|EMBL:EXI88517.1}; KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399}; KW Reference proteome {ECO:0000313|Proteomes:UP000022141}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00399}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00093725}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464105}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00399}. FT TRANSMEM 191 218 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 238 261 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 273 296 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 317 347 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 359 383 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 395 412 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 448 469 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT DOMAIN 467 608 Thioredoxin. {ECO:0000259|PROSITE: FT PS51352}. FT DISULFID 138 144 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT DISULFID 524 527 Redox-active. {ECO:0000256|HAMAP-Rule: FT 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 //