ID A0A096AND0_9BURK Unreviewed; 362 AA.
AC A0A096AND0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=HMPREF2130_01350 {ECO:0000313|EMBL:KGF32142.1};
OS Oligella urethralis DNF00040.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Oligella.
OX NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF32142.1, ECO:0000313|Proteomes:UP000029629};
RN [1] {ECO:0000313|EMBL:KGF32142.1, ECO:0000313|Proteomes:UP000029629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00040 {ECO:0000313|EMBL:KGF32142.1,
RC ECO:0000313|Proteomes:UP000029629};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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:KGF32142.1}.
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; JRNI01000006; KGF32142.1; -; Genomic_DNA.
DR RefSeq; WP_036557332.1; NZ_JRNI01000006.1.
DR AlphaFoldDB; A0A096AND0; -.
DR eggNOG; COG0526; Bacteria.
DR eggNOG; COG1999; Bacteria.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000029629; Unassembled WGS sequence.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000029629};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..362
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001924843"
FT DOMAIN 205..360
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 56
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 60
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 151
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 56..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 362 AA; 39517 MW; 731B05B2C0516BD7 CRC64;
MIRAFFIKSL VCFLAFLSGT VYAQSIRFDL FDNKGPVSHE SYPGKYLLMA IGYTSCPDIC
PTTLYEFGAV MRAIKNPDAI QPLFVTIDPT NDEVNRLNAY TGFFDKRIVG LSGTKENIKH
FADQLGATYG YSLHGKRIED PAPGMSYAVY HSALIYLIGP DRELLDVYDY QIGVEGLVEA
LDEVLGSPEA EANPGSAMLS ARQTSEAAVR APAKVTPALN CELPEGFVES KEAHELSTLL
DSAPASRVSL LNLWATWCAP CRVELPILDT FAGSQNDMSV IALNLNEPTE RVAEFFKAQA
IKNLQPQRSE DNALLRRLGG IGLPFNALFV DGQAVAIKNG VIKETEGLSH YAQCVKAHAV
SQ
//
