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Database: UniProt
Entry: A0A0Q7SR14_9BURK
LinkDB: A0A0Q7SR14_9BURK
Original site: A0A0Q7SR14_9BURK 
ID   A0A0Q7SR14_9BURK        Unreviewed;       314 AA.
AC   A0A0Q7SR14;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:KQY86071.1};
GN   ORFNames=ASD35_20820 {ECO:0000313|EMBL:KQY86071.1};
OS   Pelomonas sp. Root1444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY86071.1, ECO:0000313|Proteomes:UP000051648};
RN   [1] {ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY86071.1, ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|EMBL:KQY86071.1,
RC   ECO:0000313|Proteomes:UP000051648};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQY86071.1}.
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DR   EMBL; LMFP01000011; KQY86071.1; -; Genomic_DNA.
DR   RefSeq; WP_056875215.1; NZ_LMFP01000011.1.
DR   AlphaFoldDB; A0A0Q7SR14; -.
DR   STRING; 1736464.ASD35_20820; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000051648; Unassembled WGS sequence.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd02956; ybbN; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051648}.
FT   DOMAIN          1..111
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   314 AA;  34134 MW;  9BE627AAD815FC85 CRC64;
     MIDITLQNFE AELITASQQR PVLLDIWAPW CGPCRTLGPV LEKLEEAYAG RFTLAKLNSD
     EVPEIATQLS QMFGVRSIPF CVMFAGGQPV DGFVGALPEA QIREFLDKHV PPGEMLEAEA
     DVAEAEDLMA EGDLEAALQK LAHAVQTDPG NDAARFDYIK ALLEMGLVAE AREAFAPVAV
     KAADTLVPSP RLAALATWLQ AYEAEADPVA LQAAIAANKR DFEARFALAQ HHLAGQRFTE
     AMDELLEIIM RDKAWNGEAA RKTYVAILEL LTKPAPKPAA EAKTGTLELA GKAAIVHSDP
     LIDSYRRKLS MALF
//
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