ID A0A0J0Y4N0_9SPHI Unreviewed; 470 AA.
AC A0A0J0Y4N0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Beta-lactamase {ECO:0000313|EMBL:KLT65194.1};
GN ORFNames=AB669_16075 {ECO:0000313|EMBL:KLT65194.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT65194.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT65194.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT65194.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-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:KLT65194.1}.
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DR EMBL; LECU01000006; KLT65194.1; -; Genomic_DNA.
DR RefSeq; WP_047800271.1; NZ_LECU01000006.1.
DR AlphaFoldDB; A0A0J0Y4N0; -.
DR STRING; 1663685.AB669_16075; -.
DR PATRIC; fig|1663685.3.peg.3367; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000036014; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT DOMAIN 267..358
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 372..460
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 470 AA; 51650 MW; 2BBBC4374812A327 CRC64;
MKIEQIYTGC LAEAAYYIES DGEAAIIDPL REVETYIKKA EKAGAKIKYI FETHFHADFV
SGHVDLAEKS GARIIYGPTA KTEFDSHIAQ DGEQFKIGHL TITALHTPGH TLESTTYLLT
DESGKDHCIF SGDTLFIGDV GRPDLAQKGD LTMEDLAGML YDSLNEKIKP LADDVIVYPA
HGAGSACGKS MSKETFDSLG HQKQVNYALK AQTKEQFITE VTDGILPPPQ YFAKNAAINK
GEIESIDNVY QKGLNPLMPQ AFEDTANQTG AILLDTRDPQ VFAKGFIPNS INIGLNGQFA
PWVGALITDL KQPILLVTDQ DKEEETITRL TRVGYDSTIG YLEGGFERWT DSGKEIDTIE
SISAEAFELA AEENDITALD VRKPGEYESE HLEFTLSRPL DFINDWTNEI DPKSTYYIHC
AGGYRSMIAA SILKSRGIEN VIDIAGGYGA IKNTGLKRTD FACPSKAMKV
//
