ID F4G6V7_ALIDK Unreviewed; 198 AA.
AC F4G6V7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:AEB86569.1};
GN OrderedLocusNames=Alide2_4254 {ECO:0000313|EMBL:AEB86569.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB86569.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB86569.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB86569.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002657; AEB86569.1; -; Genomic_DNA.
DR RefSeq; WP_013723082.1; NC_015422.1.
DR AlphaFoldDB; F4G6V7; -.
DR STRING; 596154.Alide2_4254; -.
DR KEGG; adk:Alide2_4254; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_076204_3_0_4; -.
DR OrthoDB; 9781543at2; -.
DR Proteomes; UP000007938; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR047262; PRX-like1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43640; OS07G0260300 PROTEIN; 1.
DR PANTHER; PTHR43640:SF1; THIOREDOXIN-DEPENDENT PEROXIREDOXIN; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007938};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..198
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003313439"
FT DOMAIN 24..175
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 198 AA; 21119 MW; 626FFD6F2970E441 CRC64;
MQALRRTLIA LPLLLAALGA HAAAAVGQIA PDFTLQSTEG KPVRLSELRG KYVVLEWTNP
GCPFVRKHYD SGNMPATQKA AREQGLAWLS INSTAKASGD YLEPARLAER KAQPTAILMD
EEGTMGHAYG ARTTPHMYVI DPGGTLVYAG GIDSIPSARV ADIERATNYV KVALADIAAQ
RPIAAAATQP YGCSIKYK
//
