ID A0RED9_BACAH Unreviewed; 483 AA.
AC A0RED9;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Hydroxyacylglutathione hydrolase {ECO:0000313|EMBL:ABK85582.1};
GN OrderedLocusNames=BALH_2284 {ECO:0000313|EMBL:ABK85582.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK85582.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK85582.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK85582.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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DR EMBL; CP000485; ABK85582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RED9; -.
DR KEGG; btl:BALH_2284; -.
DR HOGENOM; CLU_030571_7_1_9; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00158; RHOD; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
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; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABK85582.1}.
FT DOMAIN 292..317
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 390..478
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 483 AA; 54670 MW; 274E722198DBF602 CRC64;
MEGIAMLLKY FYDEKLAHAS YLVGCQKEGV AIVIDPGRYI EQYIEFAKKE GMEVTAAAET
HIHADFLSGS RELSILYHAN LYISDEGDCD WKYQYLNEGQ YNLVREGTEF KVGHIKFSVI
HTPGHTPESI SFLVTDTSQN NYTNDKPIGI FTGDFIFVGD IGRPDLLETA VGMKDTAKIG
AKQLFDSIQK IKTLPDYLQI WPSHGAGSAC GKALGAIPTS TLGYEKMFNW AFQCNEESDF
ISTLLTGQPE PPRYFSLMKN LNKYGPPIRK KREIFAIKTV EELQEVMRSV QQIVDIRDVE
SFASGHIEKS INIPYNNSFT TWCGWLLDYK TETLIILDEE KVRVEEVIRD FESIGLDNSI
AFAPLQVIQR LDRFESYKEK TSIELYPHIK DGRVKVIDVR SKKEWDEGHL HDAIHIPLGN
LLKQLDCIPK DCPIVLQCRT GLRSAIAASI LQRAGIKGVV NLKGGFLAWK KEELPYITCS
FNV
//
