GenomeNet

Database: UniProt
Entry: A0A0S8HVP1_9DELT
LinkDB: A0A0S8HVP1_9DELT
Original site: A0A0S8HVP1_9DELT 
ID   A0A0S8HVP1_9DELT        Unreviewed;       474 AA.
AC   A0A0S8HVP1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:KPK89302.1};
GN   ORFNames=AMJ94_12435 {ECO:0000313|EMBL:KPK89302.1};
OS   Deltaproteobacteria bacterium SM23_61.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK89302.1, ECO:0000313|Proteomes:UP000051218};
RN   [1] {ECO:0000313|EMBL:KPK89302.1, ECO:0000313|Proteomes:UP000051218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_61 {ECO:0000313|EMBL:KPK89302.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK89302.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJUR01000123; KPK89302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8HVP1; -.
DR   STRING; 1703399.AMJ94_12435; -.
DR   PATRIC; fig|1703399.3.peg.1509; -.
DR   Proteomes; UP000051218; 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:KPK89302.1}.
FT   DOMAIN          262..353
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          368..456
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   474 AA;  50890 MW;  79D001D0F69BC36F CRC64;
     MFVQSFFVPG LAHLSYLLGG KSTCAIVDPR RDVDEYLSAA KNMGMGITHI LETHLHADFV
     SGHMDLAART GAEIIAPRAG KCSFPHRPVA EGDEFQIEDM SIRVLDTPGH TPEHITFVVT
     DQSRGAEPAA IFCGDTLFVG DVGRPDLFPD QAVELAGKLY QSLGKLKALP DPTLVLPAHG
     AGSLCGRAMG AMRFSAVGYE KHYNRELQHK TLDAFRGSLL TGLPEAPDHF SRCSDINRKG
     PAKVESLEAA RPLSAQEVYQ WTQKSAVVLD ARDFLAFGGA HIPGGWNIDM AGNYQTFSGW
     VIPPDQPIVL VLESDGRLLD ATTMLRRVGL DKVIGWLDGG MPSWNVAGLP EEHVPQISAQ
     ELAAVLAKDS KSAVLDVRGK LEFETLHLNG AVNIPAPDLR KRHAEVPKDR TVYVICNSGH
     RSSLACSILL QKGFKNITNV VGGMMAFSAA GLVGTCPICS APHLPAVQGA QGGK
//
DBGET integrated database retrieval system