ID B1LYL8_METRJ Unreviewed; 304 AA.
AC B1LYL8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:ACB22845.1};
GN OrderedLocusNames=Mrad2831_0835 {ECO:0000313|EMBL:ACB22845.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB22845.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB22845.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; CP001001; ACB22845.1; -; Genomic_DNA.
DR RefSeq; WP_012317838.1; NC_010505.1.
DR AlphaFoldDB; B1LYL8; -.
DR STRING; 426355.Mrad2831_0835; -.
DR KEGG; mrd:Mrad2831_0835; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_046120_1_1_5; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000006589; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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; IPR005746; Thioredoxin.
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 NCBIfam; TIGR01068; thioredoxin; 1.
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 PRINTS; PR00421; THIOREDOXIN.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..126
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 304 AA; 32243 MW; 5FB566933CFDD190 CRC64;
MLNDTLAAGG APAGDTGSLI KDTTTASFRQ DVIAESMHRP VLVDFWAPWC GPCKQLTPVL
EKVVREAAGA VVLAKMNIDE HPSIAGQLGI QSIPAVIVFQ KGQPVDGFMG AVPESQIKEL
IGRVAGPQQD PLEAALADAA ALIQEGDLAG AAEIYAAVLE QQPDNVTALA GLAKMQLDAG
EIENAKRVLA MVPEAKAGDP ALVGIRAALE LAEQAASLGD LAGLQREVEA NPDAHQARFD
LALGLAARGE RGQAVDHLIE LRKRDKDWNE DGARKQLLQF FEAWGVMDPD TIRGRRKLSA
LLFS
//
