ID Q1DA46_MYXXD Unreviewed; 765 AA.
AC Q1DA46;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:ABF86132.1};
GN OrderedLocusNames=MXAN_2256 {ECO:0000313|EMBL:ABF86132.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86132.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86132.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; CP000113; ABF86132.1; -; Genomic_DNA.
DR RefSeq; WP_011552332.1; NC_008095.1.
DR AlphaFoldDB; Q1DA46; -.
DR STRING; 246197.MXAN_2256; -.
DR EnsemblBacteria; ABF86132; ABF86132; MXAN_2256.
DR GeneID; 41359644; -.
DR KEGG; mxa:MXAN_2256; -.
DR eggNOG; COG0526; Bacteria.
DR eggNOG; COG2849; Bacteria.
DR HOGENOM; CLU_020670_0_0_7; -.
DR OrthoDB; 5481772at2; -.
DR Proteomes; UP000002402; Chromosome.
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 Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 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:SF40; THIOREDOXIN 2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 119..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 85302 MW; 634B4262C1A116A3 CRC64;
MAGQTVELTQ ENFERITQEA GVCVVDFWAE WCGPCRGFAP TFEAAAKEFP NITFGKLDTE
AQEEVSGRME IRSIPTLVAF KDGVEVRRAS GAMSASAFAT WLSKLDSVDL AVEQQRAANR
KLTEEGTPPP GIPPHAEWDA GDEEWCSGDT DEEGEKHGPW KYWRADGTLC NECIFVHGKP
HGPFKRFHES GEVSQDGAFE QGNLHGPRTW YASDQFTTER MHENGVSEKV RRTVMVYANG
RVTQVLHYNG AGERVVPSTG EPYPTRPANL PEKAEYREDQ DQWASVSLNA KAERHGLCRF
WDREGQLLWE CEFHEGSRHG RYHSRAVDEY ADPRVRFDEG EMEDDFACGT WKLLDAEGNA
VVTRDLGVVQ DHETLDASEV FSNLPRSAAE WRAFAEQARA DRRYREALLA MARASAVSLD
AGPLKAWLES LTLPRTEASA RENAEGVMNS AGDERAALAD AMMRGAEAAM LLRGFAVLHD
QQDRPRAALD FILAAMLLAP ERSAYLFTRS LILANLGLGE QMQKDAEALA PAEPDSWKFL
SAYRRVLFPR FEFWPGREPA HCTFDEVPDG PTKELDAVQA VVRKYATRLQ LLRAEILSRF
KPGTNVPWLP PDVSSLLPDG PVELEQTEVE DADGDSVDVD ETLSTKGMGI PALSRAARGD
WSALTWLLWA CGVDSIRMPD ALTPPADFGQ AAGQATQRLW QCRNRRSRGR IDPDLPTFDF
EGVALQELHP NLAGIAEEQY AETQAMFFWL TDANHVSPWQ ANLRG
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