ID F9ZIL3_9PROT Unreviewed; 645 AA.
AC F9ZIL3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=NAL212_0173 {ECO:0000313|EMBL:ADZ25130.1};
OS Nitrosomonas sp. AL212.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25130.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ25130.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ25130.1,
RC ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
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DR EMBL; CP002552; ADZ25130.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZIL3; -.
DR STRING; 153948.NAL212_0173; -.
DR KEGG; nit:NAL212_0173; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_2_0_4; -.
DR Proteomes; UP000001629; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001629};
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..20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT CHAIN 21..645
FT /note="Thiol:disulfide interchange protein DsbD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT /id="PRO_5009012542"
FT TRANSMEM 220..252
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 264..287
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 299..322
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 343..373
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 385..408
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 420..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 444..462
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DOMAIN 501..645
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 239..361
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 560..563
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ SEQUENCE 645 AA; 69715 MW; 98BAC21A89280A7F CRC64;
MRLLQFLLLI VCLSCPQAFA QESGSFSLFQ KLQGLGINLG QSNPQELLPP DEAFKISVEV
RDGNTLIAHL TPAKDYYLYR DKIAFEPKQE GMVIEKVMLP SGKMKEDMTF GNTEVYYSPV
QAIISLTRTH PASEQPLTLE ATYQGCNEPV GVCYAPIHKA IDLTLPAVKA AIGAIAGAVS
SQATAAGVDT TAELFQMPSR SPAIETESYK IERMFETGDY WLILSGFFVV GLFLSFTPCV
FPMFPILSGI IANHGKHVTK RHGFLLALAY VLGMAITYAI AGVAAGLSGA MLSAALQNAW
VLGTFAVIFV LLSFSMFGFY ELQLPGTLQT RLSEEAGLLK GGHLTSVFGM GALSALIVGP
CVAAPLAGAL LYISQTRDVV LGGSALFVMA LGMGVPLLLL GTSAGALLPK AGAWMESIKR
FFGVLLLAVA IWIISPVINE VVYMLLWAVL LIISAIYLQA IDPLPQRASG LQKFFKGVGV
IALLVGIALL IGVLSGSRDV LQPLSKLNLA DATNPGFGET VPAGYATLPF QRVKTIAELD
EQIQLSRDKY IMVRFHADWC VSCKEMDRFT FSDAKVQARL KEVVLLEVDV TEGTPDDTAL
LRRFKLFGPP GILFIDRQGY DIPDIKIIGF LNNNDFLTVL NAVLI
//
