ID A0A1N7SBZ2_9BURK Unreviewed; 618 AA.
AC A0A1N7SBZ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:SIT44917.1};
GN ORFNames=BN2476_440031 {ECO:0000313|EMBL:SIT44917.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT44917.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT44917.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT44917.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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}.
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DR EMBL; CYGY02000044; SIT44917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7SBZ2; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000195569; 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; IPR012336; Thioredoxin-like_fold.
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; 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 {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}; 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 195..228
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 240..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 276..300
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 320..349
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 361..384
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 396..414
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 420..437
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 449..471
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DOMAIN 481..614
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 133..139
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 215..337
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 531..534
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ SEQUENCE 618 AA; 64909 MW; 3804A2F75F118F0E CRC64;
MFNSFSCRWL DTARFLVLVA GVLLLSLFRV SCAHADDFLD PAVAFRFSAS EQPGEVLVHY
TIADGYYMYR ERFAFAKRDG TVTIGDPQLP AGHVKFDQTF AKNVETYRGE LTIRVPVKQA
SGPFDLAVTS QGCADAGICY PPMERVYHVT GTALHAAAAG VVGDGKNVQG TQSGASWYER
ATSADYAQSL LQGGGFFAIV GLYFVAGVVL SLLPCSYPMI PILSAIIIGE GPRVTRSRGF
ALSLAYVVGM ALVYTVLGIA AALVGQSLGA WLQNPWVLGA FALVLTVFAL TLIAGVDIVL
PQRWQSGVSK ASEGRSGGKF AAVAVMGALS ALVVGACMTA PLFAVLAFIA HTGNAVLGGA
ALFSMGIGLG VPLLIIGLGA GTLLPRAGAW MDSVKVFFGV VLLAAALWIV WPVLGATAQM
LLAALWLLIA AAGLGLFSPH AGAKSIWGGL GRGIGAALAI WAATLLVGLA AGSTNPLQPL
AVLASRTPNT PSTAAPQGDL AFAPVRSSGQ LDEAVKTAAQ PAMLDFYADW CVSCKEMEKL
TFSDPRVQAK LKQMNLLRAD VTANNADDRA LLKRFNLFGP PGIIFFDRGG REVLRVVGYE
SADKFLRSLD RVATAPQT
//