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Database: UniProt
Entry: D2R248_PIRSD
LinkDB: D2R248_PIRSD
Original site: D2R248_PIRSD 
ID   D2R248_PIRSD            Unreviewed;       489 AA.
AC   D2R248;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ADB18659.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Psta_4005 {ECO:0000313|EMBL:ADB18659.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB18659.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB18659.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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DR   EMBL; CP001848; ADB18659.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2R248; -.
DR   KEGG; psl:Psta_4005; -.
DR   eggNOG; ENOG5033UU8; Bacteria.
DR   HOGENOM; CLU_557638_0_0_0; -.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
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:UP000001887}.
FT   DOMAIN          325..486
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   489 AA;  53135 MW;  EBF2B8750F5B3817 CRC64;
     MGRRLSISLL KAFIQSFCRS YPARLLPRPA QPSIRHGSFS KAFRVLTTLV LLATLAANPQ
     IAAGEQLTYE LTITADKDDG TPQVKRIQLN LLVEQIAGEN ATVGWSLAEE GRGTFSWLEH
     YGRASVNLLE PGDSVGGPAV LLTHSGGRSV VPIAIPLAST TLSRDEGAMW TAGGLNYKTL
     ATGKRQEIDA VEIESRGRFG HRRSFWIAAE DCLMLDGVET LFVGQGEQQQ LKFKLVSRAT
     LASSDSQEAS QELDQWIALR DLLKREVRTE RPELSAEQLT TLKTELPKLI DSQKSLLLKQ
     VATSADKEVR GQKSQQAAIA ALREAILGKE AGDLTLVDLL GKVTEGESYA GKVVVLHFWK
     YTDSPLEEPY GQIGYLDFLA RKRAADGVVT LGVHCDPELS DAETRRGSLS AARRLRSFMN
     LSYPIMVDDG KLLDRLGDPR SAGAALPLFV VIGKDGKVTT YHAGLYEVNP REGLAELSTA
     ISAAVGAKP
//
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