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Database: UniProt
Entry: A8F9H5_BACP2
LinkDB: A8F9H5_BACP2
Original site: A8F9H5_BACP2 
ID   A8F9H5_BACP2            Unreviewed;       375 AA.
AC   A8F9H5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN   OrderedLocusNames=BPUM_0193 {ECO:0000313|EMBL:ABV60892.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV60892.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV60892.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV60892.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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DR   EMBL; CP000813; ABV60892.1; -; Genomic_DNA.
DR   RefSeq; WP_012008769.1; NZ_VEIA01000007.1.
DR   AlphaFoldDB; A8F9H5; -.
DR   STRING; 315750.BPUM_0193; -.
DR   KEGG; bpu:BPUM_0193; -.
DR   eggNOG; COG0491; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_030571_7_2_9; -.
DR   OrthoDB; 9784009at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044528; POD-like_MBL-fold.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR43084:SF7; BETA-LACTAMASE DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
FT   DOMAIN          17..112
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   375 AA;  41887 MW;  11542988C3FC2FF8 CRC64;
     MTVKAMTAEQ LTKKIVNKEP LFLLDVRNQA DVQDWKIEGE AIVHMNVPYF DLLEGVEGIL
     HDIPHDREVL VVCAKEGSSI MVAEMLSEAG RTVHYLEGGM KAWSEHLEPV KIGDLSGGGE
     LYQFVRMGKG CLSYMIMSNG ESAIVDAARM TDVYIRFAKK HHVSITQVLD THLHADHISG
     GKKLAEQTGA SYWLPPKDAE EVIFEYNRLE EGERIAIGAA TIDIHPLYSP GHTIGSTSFI
     VDDQYLLSGD ILFVDSIGRP DLAGMAEDWA GDLRETLYDR YGALSKELIV LPAHFMIMDE
     VNEDGSVWKE LGVLFEENHG LNIEDEAVFR EMVTKNLPAQ PNAYQDIRQT NMGKLSPDDE
     AQREMEIGPN RCAIR
//
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