ID A0A0P7WFX5_9RHOB Unreviewed; 106 AA.
AC A0A0P7WFX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN Name=trxA-2 {ECO:0000313|EMBL:KPP89212.1};
GN ORFNames=HLUCCA08_03205 {ECO:0000313|EMBL:KPP89212.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP89212.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KPP89212.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP89212.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(2016).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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:KPP89212.1}.
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DR EMBL; LJSF01000016; KPP89212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WFX5; -.
DR STRING; 1666913.HLUCCA08_03205; -.
DR PATRIC; fig|1666913.4.peg.2355; -.
DR Proteomes; UP000050293; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 25
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 106 AA; 11399 MW; AA5A80DF3F22FB28 CRC64;
MATVAVTDDT FDAEVRQSDI PVVVDFWAEW CGPCKMIGPA LEELSTELDG KVKIVKVDVD
QNPNSPAQLG VRGIPALFIF KDGEVISNRA GAAPKAALQS WINDSI
//