ID A0A0T0M3V2_9FLAO Unreviewed; 469 AA.
AC A0A0T0M3V2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:KQS89949.1};
GN ORFNames=ASG21_13315 {ECO:0000313|EMBL:KQS89949.1};
OS Chryseobacterium sp. Leaf394.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1736361 {ECO:0000313|EMBL:KQS89949.1, ECO:0000313|Proteomes:UP000051822};
RN [1] {ECO:0000313|EMBL:KQS89949.1, ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|EMBL:KQS89949.1,
RC ECO:0000313|Proteomes:UP000051822};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
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:KQS89949.1}.
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DR EMBL; LMQH01000012; KQS89949.1; -; Genomic_DNA.
DR RefSeq; WP_056082811.1; NZ_LMQH01000012.1.
DR AlphaFoldDB; A0A0T0M3V2; -.
DR STRING; 1736361.ASG21_13315; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000051822; 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:KQS89949.1}.
FT DOMAIN 268..359
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 372..460
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 469 AA; 51933 MW; BBA5564018068976 CRC64;
MKIEQIYTGC LAQGAYYIVS GNEAAIIDPL REVKPYLDRL EKDNVTLKYI FETHFHADFV
SGHLDLSKKT DAPIVYGPTA KPEFEAIIAE DNQIFEIGNI KIKALHTPGH TMESTTYLLI
DENGIETAIF TGDTLFLGDV GRPDLAQKAG TMTQEDLAGI LYESLHSKIL PLDDSITVYP
AHGAGSACGK NMQKETVDIL GNQRKTNYAL NQPDKESFIK EVLDGLTAPP KYFGMNVAMN
KNGYESLDDV MDKGLNPISV EDFESFAEET GALILDTRGP AEFHKGFIPN SINIGLKGDF
APWVGSLIVD VKHPLLLVAD EGTEEEVITR LSRVGFDNVV GYLKGGFSSW KNSTKEIDEV
KRITPTEFVE QFNEHSKIID VRKIGEYSAE HIDNAYSRPL DTISDWVSTV DDSEHFFLHC
AGGYRSMIAA SILNSHGIRN FTEIEGGFNG IKKTEKLPVS DFVCQSKML
//
