ID E6MNX9_9BACT Unreviewed; 163 AA.
AC E6MNX9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:EFV04566.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:EFV04566.1};
GN Name=trxA {ECO:0000313|EMBL:EFV04566.1};
GN ORFNames=HMPREF9420_1197 {ECO:0000313|EMBL:EFV04566.1};
OS Segatella salivae DSM 15606.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV04566.1, ECO:0000313|Proteomes:UP000003874};
RN [1] {ECO:0000313|EMBL:EFV04566.1, ECO:0000313|Proteomes:UP000003874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV04566.1,
RC ECO:0000313|Proteomes:UP000003874};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFV04566.1}.
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DR EMBL; AEQO01000115; EFV04566.1; -; Genomic_DNA.
DR RefSeq; WP_007134465.1; NZ_GL629647.1.
DR AlphaFoldDB; E6MNX9; -.
DR STRING; 888832.HMPREF9420_1197; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_2_1_10; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000003874; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:EFV04566.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000003874};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..163
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003208582"
FT DOMAIN 37..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 163 AA; 18228 MW; 02EAF1DE3E4F39E9 CRC64;
MKKTIFLMAL TALVGLSACS SQTNSKATTE TKQNNNKQVK EKKMKVTELT TAAFKKEVMD
FDKHPNEWLF EGKRPAVIDF YATWCGPCKA TAPIVEALAE VYAGKVDFYK VDVDAQEELA
SFFGIRSIPT LLFIPQEGKP SMQVGAMNRQ QLEDAIKKTL LKQ
//
