ID I4ZAF1_9BACT Unreviewed; 165 AA.
AC I4ZAF1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:EIM33193.1};
GN ORFNames=PrebiDRAFT_1489 {ECO:0000313|EMBL:EIM33193.1};
OS Prevotella bivia DSM 20514.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33193.1, ECO:0000313|Proteomes:UP000002786};
RN [1] {ECO:0000313|EMBL:EIM33193.1, ECO:0000313|Proteomes:UP000002786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33193.1,
RC ECO:0000313|Proteomes:UP000002786};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; JH660660; EIM33193.1; -; Genomic_DNA.
DR RefSeq; WP_004337976.1; NZ_JH660660.1.
DR AlphaFoldDB; I4ZAF1; -.
DR GeneID; 78531446; -.
DR HOGENOM; CLU_090389_2_1_10; -.
DR Proteomes; UP000002786; 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 PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000002786};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 24..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 18353 MW; FDE005E462698EE3 CRC64;
MKLSAILIAL PLVIGTASCK QQPKQSAEKV ASTETKTSNN NNSGKEKKME VQEMTAQMFK
EKVMNYEKNP NTWVFEGDKP VLIDFYATWC GPCKATAPIV EELANEYAGK LDVYKVDVDK
QEELAALFGI RSIPTFLFVP KNGKPTLQSG AMSKPQFEEI LKTNI
//
