ID A1WUL2_HALHL Unreviewed; 77 AA.
AC A1WUL2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Redox-active disulfide protein 2 {ECO:0000313|EMBL:ABM61374.1};
GN OrderedLocusNames=Hhal_0588 {ECO:0000313|EMBL:ABM61374.1};
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61374.1, ECO:0000313|Proteomes:UP000000647};
RN [1] {ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABM61374.1, ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX PubMed=23991253; DOI=10.4056/sigs.3677284;
RA Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT "Complete genome sequence of Halorhodospira halophila SL1.";
RL Stand. Genomic Sci. 8:206-214(2013).
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DR EMBL; CP000544; ABM61374.1; -; Genomic_DNA.
DR RefSeq; WP_011813397.1; NC_008789.1.
DR AlphaFoldDB; A1WUL2; -.
DR STRING; 349124.Hhal_0588; -.
DR KEGG; hha:Hhal_0588; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_090389_18_1_6; -.
DR OrthoDB; 9800630at2; -.
DR Proteomes; UP000000647; Chromosome.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR005243; THIRX-like_proc.
DR NCBIfam; TIGR00412; redox_disulf_2; 1.
DR PANTHER; PTHR36450; THIOREDOXIN; 1.
DR PANTHER; PTHR36450:SF1; THIOREDOXIN; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037031-51};
KW Redox-active center {ECO:0000256|PIRSR:PIRSR037031-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT DOMAIN 3..77
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT DISULFID 11..14
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ SEQUENCE 77 AA; 8190 MW; 2A9E9218F43D058F CRC64;
MKAIKVLGSG CAKCNNTAER IEQVAADLGL AAQVQKETGP EALVQYGVMS TPAVVVDEQL
VHSGSVPEPE QIKEWLQ
//
