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Database: UniProt
Entry: A0A0Q4GLX1_9SPHI
LinkDB: A0A0Q4GLX1_9SPHI
Original site: A0A0Q4GLX1_9SPHI 
ID   A0A0Q4GLX1_9SPHI        Unreviewed;       470 AA.
AC   A0A0Q4GLX1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:KQM74701.1};
GN   ORFNames=ASE74_01560 {ECO:0000313|EMBL:KQM74701.1};
OS   Pedobacter sp. Leaf216.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM74701.1, ECO:0000313|Proteomes:UP000051744};
RN   [1] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Garrido-Oter R., Mueller D.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQM74701.1}.
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DR   EMBL; LMKM01000012; KQM74701.1; -; Genomic_DNA.
DR   RefSeq; WP_055908091.1; NZ_LMKM01000012.1.
DR   AlphaFoldDB; A0A0Q4GLX1; -.
DR   STRING; 1735684.ASE74_01560; -.
DR   OrthoDB; 9784009at2; -.
DR   Proteomes; UP000051744; Unassembled WGS sequence.
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; 2.
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:KQM74701.1}.
FT   DOMAIN          267..358
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          372..460
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   470 AA;  51358 MW;  6051C42E585CBF55 CRC64;
     MKIEQIYTGC LAEAAYYIES DGEAAIIDPL REVGTYLKKA EKAGATIKYI FETHFHADFV
     SGHVDLAEKS GAEIIYGPTA KTEFKAHIAQ DGEQFKVGRV TITALHTPGH TLESTTYLLT
     DENGKDHCIF SGDTLFIGDV GRPDLAQKGH LTMEDLAGML YDSLNEKIKP LADDVIVYPA
     HGAGSACGKS MSKETFDTLG HQKEVNYALK AQTKEQFITE VTDGIMPPPQ YFAKNAAINK
     GGVESIDEVY EKGLNALTPQ QFEDTANQTG AIMLDTRDPQ VFAKGFIPNS INIGLNGQFA
     PWVGALISDL QQPILLITDE GKEEETITRL TRVGYDSTIG YLDGGFERWT DAGKEIDTID
     SISAEAFEEA NTNGEITALD VRKPGEYESE HLEFTLSRPL DFINEWTGEI DPKSTYYIHC
     AGGYRSMIAA SILKSRGVEN VIDVAGGYAA IKNTGLKRTD FACPSKAMKV
//
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