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Database: UniProt
Entry: D4GI32_PANAM
LinkDB: D4GI32_PANAM
Original site: D4GI32_PANAM 
ID   D4GI32_PANAM            Unreviewed;       564 AA.
AC   D4GI32;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   20-JUN-2018, entry version 63.
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   ECO:0000313|EMBL:ADD75562.1};
GN   OrderedLocusNames=PANA_0395 {ECO:0000313|EMBL:ADD75562.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD75562.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD75562.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD75562.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R.,
RA   Joubert F., Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(2010).
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: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H. {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}.
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DR   EMBL; CP001875; ADD75562.1; -; Genomic_DNA.
DR   RefSeq; WP_013024295.1; NC_013956.2.
DR   ProteinModelPortal; D4GI32; -.
DR   STRING; 706191.PANA_0395; -.
DR   EnsemblBacteria; ADD75562; ADD75562; PANA_0395.
DR   GeneID; 31509335; -.
DR   KEGG; pam:PANA_0395; -.
DR   eggNOG; ENOG4105CSG; Bacteria.
DR   eggNOG; COG4232; LUCA.
DR   HOGENOM; HOG000254981; -.
DR   KO; K04084; -.
DR   OMA; FVYVQGM; -.
DR   OrthoDB; POG091H0F5X; -.
DR   BioCyc; PANA706191:PANA_RS02070-MONOMER; -.
DR   Proteomes; UP000001702; Chromosome.
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   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:SF0; PTHR32234:SF0; 1.
DR   Pfam; PF11412; DsbC; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF13098; Thioredoxin_2; 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:UP000001702};
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:SAAS00093715};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00464121};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093729};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   SIGNAL        1     23       {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   CHAIN        24    564       Thiol:disulfide interchange protein DsbD.
FT                                {ECO:0000256|HAMAP-Rule:MF_00399}.
FT                                /FTId=PRO_5009009520.
FT   TRANSMEM    167    193       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    205    230       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    242    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    289    316       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    328    350       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    362    380       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    386    405       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DOMAIN      433    564       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID    126    132       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    181    303       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    479    482       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
SQ   SEQUENCE   564 AA;  61255 MW;  91DE2511A533F746 CRC64;
     MAARISRLIT LVLALFICLQ AQAALFSPKT TSRFLPVDQA FAFDFDQQGS QLNLHWKVKE
     GYYLYRQQIK VVPHDARIAP LALPAGQPHE DEFFGKSEIY PQDLNVPIML QQAAKGATLS
     VSYQGCAAAG FCYPPETRSI PLSPVAATMS PPAVAPASAN PLPFSPLWAL LIGIGVAFTP
     CVLPMYPLIS GIILGGKRNY SLGRLFALAM VYVQGMALTY TLLGVIVAAA GLRFQAALQH
     PYVLIGLSAL FTLLALSMFG LFSLQLPASV QTRLALWSNR QQGGSLPGVF LMGALAGLIC
     SPCTTAPLSA ILLYIAQSGN LLAGAGTLWL YAVGMGLPLI AVTLFGNRFL PKSGPWMQTV
     KEGFGFVILA LPVFLLERIL GDLWGMRLWS LLAVAFFAWA FSASLRASGG KWRVMQIMML
     VAALISARPL QDWAFGSGAP QQNIAHLPFQ PVQTLEQVDQ ALQQAQGRIT MVDLYADWCV
     ACKEFEKYTF SDSAVRDNLN NVQLLQANVT ANTATDNALL QHLHVLGLPT ILFFDATGKE
     IPESRITGFL KANDFRAHLQ KLHE
//
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