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Database: UniProt
Entry: A0A0M2XWY5_9SPHI
LinkDB: A0A0M2XWY5_9SPHI
Original site: A0A0M2XWY5_9SPHI 
ID   A0A0M2XWY5_9SPHI        Unreviewed;       465 AA.
AC   A0A0M2XWY5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:KKO90154.1};
GN   ORFNames=AAW12_16620 {ECO:0000313|EMBL:KKO90154.1};
OS   Sphingobacterium sp. Ag1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO90154.1, ECO:0000313|Proteomes:UP000034524};
RN   [1] {ECO:0000313|EMBL:KKO90154.1, ECO:0000313|Proteomes:UP000034524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKO90154.1,
RC   ECO:0000313|Proteomes:UP000034524};
RA   Pei D., Yu W., Kukutla P., Xu J.;
RT   "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-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:KKO90154.1}.
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DR   EMBL; LBGU01000042; KKO90154.1; -; Genomic_DNA.
DR   RefSeq; WP_046674782.1; NZ_LBGU01000042.1.
DR   AlphaFoldDB; A0A0M2XWY5; -.
DR   PATRIC; fig|1643451.3.peg.1894; -.
DR   Proteomes; UP000034524; 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; 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; 1.
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:KKO90154.1}.
FT   DOMAIN          275..301
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          377..465
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   465 AA;  51674 MW;  08B013DB9343F981 CRC64;
     MFFQHIFESS LAHSSYIIGC QAKGVAIVID PKRDVDSYLE IAQKNNLTIT HIAETHIHAD
     YLSGTLELAA LTGAQPYLSD EGGEDWHYEF PHIGLKHGDQ FHVGNLIFQV IHTPGHTPES
     ISFVLIDTPA TMEPVMLFTG DFVFVGDIGR PDLLENAAGM VGTKEIGAHQ MYRSLQHFLT
     LPDHIQVWPA HGAGSACGKA LGAVPSSTVG YEKIRNWALQ YQNNETAFVE ELLSGQPEPP
     RYFATMKKLN KIARPLQTAV PQYNKLANET FLDLYQQGTT VIDTRYKFDF AKGYLPNSIN
     IQNNKTFNTW AGWILNYTDP FILIVAESQL DDIARKLMRI GLDQVAGYVT PDTIPHLGIA
     LEHQQLIGFE EMNSALGKSD IQILDVRNSS EFAEGHLPHA THIFVGTIAD NLHKIDQNKQ
     LYLHCQSGDR ATIAASILAK NGIKDVKIYS PSINEWKLKG GTLVQ
//
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