ID A0A014NLH8_9BURK Unreviewed; 665 AA.
AC A0A014NLH8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:EXU80318.1};
GN ORFNames=AX13_17245 {ECO:0000313|EMBL:EXU80318.1};
OS Comamonas aquatica DA1877.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU80318.1, ECO:0000313|Proteomes:UP000020766};
RN [1] {ECO:0000313|EMBL:EXU80318.1, ECO:0000313|Proteomes:UP000020766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU80318.1,
RC ECO:0000313|Proteomes:UP000020766};
RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA Caudy A.A., Walhout A.J.;
RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT Gene Expression and Life History Traits.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EXU80318.1}.
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DR EMBL; JBOK01000008; EXU80318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A014NLH8; -.
DR STRING; 225991.MA05_00400; -.
DR PATRIC; fig|1457173.3.peg.1696; -.
DR Proteomes; UP000020766; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR PANTHER; PTHR32234; 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; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000020766};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 269..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 538..665
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 665 AA; 69930 MW; B917ECA0F9AF3128 CRC64;
MVTPRVRAQL VALAPEGIAP GRPLALGLRI EHQPDWHTYW KNAGDSGLPT QLTWQLPAGL
HAGEIAWPVP QQIRVGDMLN YGYEGTVLLP VPLQVAPDFA PGSDGGVDIR LHASWLVCRV
ECIPEEGNFL MRLPASAPQT LWSAAFEAAH AQAPLALDTA QASASASDGG ERLQLRVAGL
PQAAHGQTLA LYPETADTLV HAAVLGQDWH QRWDGAVWTA DVPLSPMRGE APPQLASVSP
ALAAALAANQ QAAATLPAPP APSASTATWL LAVLGGLVGG LLLNLMPCVF PVLAIKVMGF
ARHGTDTAAQ RRHGLAYAAG VVLSFLALGG VLLGLRAAGE QLGWGFQLQS PAVVAALAAL
FTLIGLNLAG VFEFGHVLPS RVANLHARHP LGDAFLSGVV AVAIASPCTA PFMGASLGFA
VGLPAVQALS VFAALGVGMA LPYVLVSWVP ALLRWLPRPG AWMDTFRRAM AFPMFATVIW
LVWVIGQQTG IDGAATLLAL LLCLAALAWT LTLRGRTRAV LALLVLALAG WLAHSLGRNL
LEPAPVATAT SARDTWQPWS PDAQAALLTA GRPVFVDYTA AWCVTCQVNK RTTLADAEVL
ADFARRNVAL LRADWTRRDP AITQALAALG RNGVPVYVLL APGQPPVVLT ELLSRQEVHT
ALAQL
//