GenomeNet

Database: UniProt
Entry: A0A0Q6B7F7_9PROT
LinkDB: A0A0Q6B7F7_9PROT
Original site: A0A0Q6B7F7_9PROT 
ID   A0A0Q6B7F7_9PROT        Unreviewed;       598 AA.
AC   A0A0Q6B7F7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=ASG34_12020 {ECO:0000313|EMBL:KQT41453.1};
OS   Methylophilus sp. Leaf416.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT41453.1, ECO:0000313|Proteomes:UP000050891};
RN   [1] {ECO:0000313|EMBL:KQT41453.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41453.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT41453.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41453.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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: 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:KQT41453.1}.
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; LMQS01000004; KQT41453.1; -; Genomic_DNA.
DR   RefSeq; WP_055830812.1; NZ_LMQS01000004.1.
DR   AlphaFoldDB; A0A0Q6B7F7; -.
DR   Proteomes; UP000050891; 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};
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..24
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   CHAIN           25..598
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT                   /id="PRO_5008994334"
FT   TRANSMEM        180..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        224..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        308..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        339..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        381..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        404..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        434..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DOMAIN          464..594
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        131..137
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        199..321
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        510..513
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   598 AA;  64597 MW;  D99A40B23620BB4A CRC64;
     MITKWIKAWA TLAMLLATAL PVHADSRFSQ LFTDEDAEEF LPVDKAFKVE AVLVDQTHAQ
     VKFIIAPGHY LYRERIQLLP ADQKATISLP PGESKNDPNF GQQQVFHHDT AAEVVFPDTA
     PAMLQIRYQG CSEKGLCYPP QTKSLPLTPS ASPVSVTSSQ PSALEVDDGV SEKLLSSGHW
     WQIVAGFFGA GLLLAFTPCV FPMIPILSGI IVGKNAQASR AKAFTLSLAY TLGMCLTYTL
     AGVAAGLSGQ LLSNALQTPW ALTAGALIFV ALSFSMFGFY ELKLPSAIEN AFFNWSHRFK
     GGHLLSDFLM GAISALIISP CVAAPLAGAL LYISQTHDVV LGAVALFSLS LGMGMPLLLI
     GASAGSILPK AGEWMNTIRR LFGVLMLAVA IWVISPILPT SVQMLLWAAL CIIPAIYLRA
     IDPLPTTAST AQRLIKGAAV FLLLYGVALL IGAWSGASSP LRPLQNLASA PQTGRQAVQF
     QRVRNVQELD QAVHAAQGKR VMLDFYADWC VSCKEYEQFV FTNHQVQAEL NQIVLLQADV
     TANNAQDAAL LKKFELFGPP GIIFFDSQGQ PLQPVIKGYH DADRFLKILR ALGGPNHA
//
DBGET integrated database retrieval system