ID Q65S27_MANSM Unreviewed; 107 AA.
AC Q65S27;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN Name=trxA {ECO:0000313|EMBL:AAU38233.1};
GN OrderedLocusNames=MS1626 {ECO:0000313|EMBL:AAU38233.1};
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38233.1, ECO:0000313|Proteomes:UP000000607};
RN [1] {ECO:0000313|EMBL:AAU38233.1, ECO:0000313|Proteomes:UP000000607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38233.1,
RC ECO:0000313|Proteomes:UP000000607};
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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DR EMBL; AE016827; AAU38233.1; -; Genomic_DNA.
DR RefSeq; WP_011200794.1; NC_006300.1.
DR AlphaFoldDB; Q65S27; -.
DR STRING; 221988.MS1626; -.
DR KEGG; msu:MS1626; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_6; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000000607; 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 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..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 26
FT /note="Deprotonates C-terminal active site Cys"
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 SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 107 AA; 11528 MW; 2184DDD7D389962C CRC64;
MSEVLHATDA SFEADVLRSD VPVLVDLWAP WCGPCRMVAP ILDDLAAELA GKVKIVKINI
DENQGTPAQF GVRSIPTLLM FKDGQLVGTQ VGALPKNQLA AFVEKNL
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