ID A0A0Q9AF23_9FLAO Unreviewed; 471 AA.
AC A0A0Q9AF23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:KRD12776.1};
GN ORFNames=ASE21_02385 {ECO:0000313|EMBL:KRD12776.1};
OS Flavobacterium sp. Root901.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD12776.1, ECO:0000313|Proteomes:UP000051400};
RN [1] {ECO:0000313|EMBL:KRD12776.1, ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|EMBL:KRD12776.1,
RC ECO:0000313|Proteomes:UP000051400};
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:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Schulze-Lefert P.;
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:KRD12776.1}.
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DR EMBL; LMJB01000001; KRD12776.1; -; Genomic_DNA.
DR RefSeq; WP_057120954.1; NZ_LMJB01000001.1.
DR AlphaFoldDB; A0A0Q9AF23; -.
DR STRING; 1736605.ASE21_02385; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000051400; 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:KRD12776.1}.
FT DOMAIN 269..360
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 374..462
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 471 AA; 51993 MW; C1554EDA82B802AE CRC64;
MKIEQIYTGC LAQGAYYITS NGEAAIIDPL REIQPYLDRL KRDNVKLKYI FETHFHADFV
SGHIDLSKET QAPIVYGPNA ACEFECISAK DGQEFKIGNV TIKALHTPGH TLESTTYLLI
DKDGKDHAIF SGDTLFIGDV GRPDLAQKAA GMTQDQLAAT LYHSLRNKIM TLADDVIVYP
AHGAGSACGK NMSKETVSTI GNQKASNYAL RANMTEAEFI KEVTDGLLPP PAYFSMNVAM
NKKGYESFET VLHNGMKTIK AEEFEAVAEE TGALILDTRK SGDFAKGFIP QSINIGINGD
FAPWVGTLVG DVRQPIILVT ENGLEEETVT RLSRVGFDSI VGHLEGGFEA WKKAGFEIDT
VNRISAEQFA NEFKFGEDKV IDIRKETEYE AEHIEDAYSK PLAYINEWVK DIDSNEHFYL
HCAGGYRSMI AASILQARGF RNFSEIDGGF GAIAKTEIPK SDFVCQSKVL K
//
