ID G7LQE2_9GAMM Unreviewed; 421 AA.
AC G7LQE2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:EHD22545.1};
GN ORFNames=BrE312_3177 {ECO:0000313|EMBL:EHD22545.1};
OS Brenneria sp. EniD312.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD22545.1};
RN [1] {ECO:0000313|EMBL:EHD22545.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD22545.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA Glasner J., Perna N., Woyke T.;
RT "Complete sequence of Brenneria sp. EniD312.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions.
CC {ECO:0000256|ARBA:ARBA00003318}.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; CM001230; EHD22545.1; -; Genomic_DNA.
DR RefSeq; WP_009113844.1; NZ_CM001230.1.
DR AlphaFoldDB; G7LQE2; -.
DR STRING; 598467.BrE312_3177; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_651877_0_0_6; -.
DR Proteomes; UP000002759; 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; 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; 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 421 AA; 47334 MW; E553E45F8C2022F6 CRC64;
MSDVIITASD ATLDNLLKNS DKPVLLDLWA PWCQPCKTLA PLLEALADNT PDDLTVAKLN
VEQYPDLMRR FGVRGIPTLL LFKDGREISR QIGVKTLPQL RGWLASHQIT VQQNAQPVTD
AAVSWGAFYG DASLHAFLHQ RLRQHAADGE IAISFSPYWQ ENKGTISAAF VHCARIEVFE
RVTGLPASLA LLLENLTCAT PRQVDALFDA VGPGKAVGDI PLQWLHLWLG DAENPWSDWL
TDRSLDDLRR QWRRLAARQA AGETVAESEW ARLHQQATAR QEKAGIEQGL EKNIAALLAI
LSPPPAPADA ASWQGIKLYL GFALAEILRI EAGWSNEERA TPDKRHLWFK KHEAAAPGKR
LTDERIAELR ARWLQENPEF SAKEDEFYRQ YPSLQEQQKA PLQEKLWRLL RNAPLCKPQP
E
//
