ID W2UMS1_9FLAO Unreviewed; 99 AA.
AC W2UMS1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:ETN95465.1};
GN ORFNames=P278_11870 {ECO:0000313|EMBL:ETN95465.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN95465.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN95465.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN95465.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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:ETN95465.1}.
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DR EMBL; AYXY01000019; ETN95465.1; -; Genomic_DNA.
DR RefSeq; WP_038263705.1; NZ_AYXY01000019.1.
DR AlphaFoldDB; W2UMS1; -.
DR STRING; 376730.SAMN04487906_2561; -.
DR PATRIC; fig|1286632.3.peg.1179; -.
DR eggNOG; COG3118; Bacteria.
DR Proteomes; UP000018850; 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 Reference proteome {ECO:0000313|Proteomes:UP000018850};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..99
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 27
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 18
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 25
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 26
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 24..27
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 99 AA; 11116 MW; 447618778C25C48B CRC64;
MKSSFKDIIN KEKPVLIDFF ATWCGPCQTL APILKETKNE LGEEVNIVKV DVDKNQPLAA
NFQVRGVPTL ILFKNGEIVW RHSGLASKND LVKVIKSHL
//
