ID   A0A0N1L7A1_9PROT        Unreviewed;       187 AA.
AC   A0A0N1L7A1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Electron transporter {ECO:0000313|EMBL:KPF61842.1};
GN   ORFNames=IP88_15395 {ECO:0000313|EMBL:KPF61842.1};
OS   alpha proteobacterium AAP81b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF61842.1, ECO:0000313|Proteomes:UP000037971};
RN   [1] {ECO:0000313|EMBL:KPF61842.1, ECO:0000313|Proteomes:UP000037971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP81b {ECO:0000313|EMBL:KPF61842.1,
RC   ECO:0000313|Proteomes:UP000037971};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF61842.1}.
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DR   EMBL; LJHX01000175; KPF61842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1L7A1; -.
DR   STRING; 1523432.IP88_15395; -.
DR   PATRIC; fig|1523432.3.peg.1264; -.
DR   Proteomes; UP000037971; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000037971}.
FT   DOMAIN          3..187
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         58
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         62
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        58..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   187 AA;  19992 MW;  CBD953374567621F CRC64;
     MLLVAGVAWL RFTAPPPGNL TGSSLGGPLA LIDQDGKRLG PDAFDGKYRL IYFGYTFCPD
     VCPTDVQVIG QGLKAFEASD AGRAAKVVPI FVTVDPERDD AKAVKAFVRA FHPRMVGLTG
     TPAEIDAVKK AYGIYARKAT TSDPANYLVD HFAVVYLFGP RGAPIAFLPH QGLTAADVTR
     LLDAQVR
//