(data stored in SCRATCH9089 zone)

SWISSPROT: DSBD_PASMU

ID   DSBD_PASMU              Reviewed;         576 AA.
AC   Q9CP40;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 125.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD;
DE            EC=1.8.1.8;
DE   AltName: Full=Protein-disulfide reductase;
DE            Short=Disulfide reductase;
DE   Flags: Precursor;
GN   Name=dsbD; OrderedLocusNames=PM0221;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- 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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK02305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE004439; AAK02305.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q9CP40; -.
DR   EnsemblBacteria; AAK02305; AAK02305; PM0221.
DR   KEGG; pmu:PM0221; -.
DR   PATRIC; fig|272843.6.peg.229; -.
DR   eggNOG; ENOG4105CSG; Bacteria.
DR   eggNOG; COG4232; LUCA.
DR   HOGENOM; HOG000254981; -.
DR   KO; K04084; -.
DR   OMA; FVYVQGM; -.
DR   Proteomes; UP000000809; Chromosome.
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   Pfam; PF00085; Thioredoxin; 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;
DR   PRODOM; Q9CP40.
DR   SWISS-2DPAGE; Q9CP40.
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..576
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /id="PRO_0000007380"
FT   TOPO_DOM        20..177
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..253
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..336
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..394
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..576
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          433..570
FT                   /note="Thioredoxin"
FT   DISULFID        120..125
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..315
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        485..488
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   576 AA;  64465 MW;  98507447D5EDFA41 CRC64;
     MKKIFFIFFL IWTSLSVNAG VFDKKNAFLK AEQAFVFTES QQNDRLSLNW DIASGYYLYK
     KSLEIKGENG QLFIPQLPLA EIHQDDFFGD VEIYRHQLTF SLPFTQLSAT KQVEITYQGC
     TEGFCYPPET RVIALTSLER ESGQISSAVL KEESVLSELP LAEQDRLAAK LIESKYAVFW
     FFLFGLGLAF TPCVLPMLPL LSAIVIGREQ RPSTAKAFGL SVVYVQGMAL TYTLLGLIVA
     AIGLPFQVAL QSPYVLLTLS AIFVLLALSM FGLFTLQLPV SLQTKLTQYS QQQKSGVFGG
     VFVMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAITL YLLALGMGLP LIFITVFGNN
     ILPKSGNWMI QVKNAFGFVL LALPIFLISR VFPEIEMPLW FSLAFAFSLW LLYQFRNNKG
     VWVFTFILGV MGYLYYSYAM NRHTPAHQTT SLSQFERITS YAQLQQVLSK NPNSLAMLDL
     YADWCVACKE FETHTFSDVA VQKAFTDVLL LQVDMTKNSE ANRELMQKLH VIGLPTLIFF
     NQQGQEIEGS RITGFMQASP FVDWLQKMKS IQPISQ
//

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