ID A0A0P7YRH9_9SPHN Unreviewed; 450 AA.
AC A0A0P7YRH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:KPP92935.1};
DE EC=3.1.2.6 {ECO:0000313|EMBL:KPP92935.1};
GN ORFNames=HLUCCO15_07245 {ECO:0000313|EMBL:KPP92935.1};
OS Erythrobacteraceae bacterium HL-111.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae.
OX NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP92935.1, ECO:0000313|Proteomes:UP000050295};
RN [1] {ECO:0000313|EMBL:KPP92935.1, ECO:0000313|Proteomes:UP000050295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-111 {ECO:0000313|EMBL:KPP92935.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP92935.1}.
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DR EMBL; LJSW01000011; KPP92935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YRH9; -.
DR PATRIC; fig|1666908.3.peg.155; -.
DR Proteomes; UP000050295; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
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; 1.
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:KPP92935.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 266..340
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 366..450
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 450 AA; 48915 MW; 7088F6D82CC3B343 CRC64;
MILETIKTTG LSHLSYLVGA GGKAAVIDPR RDCEIYLEHA RAQGLEITHI LETHRNEDLV
SGSPLLAAMT GARVLHGPNP ERPVVFAETA REGDSIDIGQ LRIEVIETPG HTDDHLAYAV
HDTAYPDGAV GVFTGDALFI GDVGRTDFYP DRKREVAGLL YDSLQKLLAL GDQAIVYPAH
GAGSVCGSGM AEREFSTIGH ERRNNPRLQF ETRDDFIAFK IAEHHYQPPY FRLMERLNMD
GADPAPRVLR PKVLSLGELH EAQCDHVIDV RDPLAFASGH LAGAMSLPTG MISAFAGWFI
GEEHRIGLVA SDEAQLNAAM EHLARIGLDR IAGGFVGVVP AAANGADMRA IPTVQTETVE
RRLAQAGEDW TLLDVRDADE RASGAIEGSQ HLYVGHLNEG WRDLDPDRHY TVMCASGMRA
TVAAGWLASR GFDRLDIYLG SMGAWSHAHG
//