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
//