ID A0A1R3KXD5_COCAP Unreviewed; 318 AA.
AC A0A1R3KXD5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Beta-lactamase-like protein {ECO:0000313|EMBL:OMP11755.1};
GN ORFNames=CCACVL1_00289 {ECO:0000313|EMBL:OMP11755.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMP11755.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMP11755.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMP11755.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
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:OMP11755.1}.
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DR EMBL; AWWV01000917; OMP11755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3KXD5; -.
DR STRING; 210143.A0A1R3KXD5; -.
DR EnsemblPlants; OMP11755; OMP11755; CCACVL1_00289.
DR Gramene; OMP11755; OMP11755; CCACVL1_00289.
DR OMA; CVWPGMR; -.
DR OrthoDB; 5471651at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR NCBIfam; TIGR03413; GSH_gloB; 1.
DR PANTHER; PTHR11935; BETA LACTAMASE DOMAIN; 1.
DR PANTHER; PTHR11935:SF7; HYDROXYACYLGLUTATHIONE HYDROLASE 2, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 75..233
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 318 AA; 34942 MW; 79F17B924451C8B7 CRC64;
MASFPCSKVR SGFCVWPGMR QLCIRKGLVY GFMRLLSTPF KTLRGASRSL RVAEFCSVSN
MSSSLQIELV PCLRDNYAYL LHDVDTGTVG VVDPSEAVPI IDALSRKNRN LTYILNTHHH
HDHTGGNAEL KARFGAKVIG SAVDKDRIPG IDIVLNDGDK WMFAGHEVHV IKTPGHTRGH
ISFYFPGSGA IFTGDTLFSL SCGKLFEGTP EQMFSSLQKI LSLPDDTNIY CGHEYTLSNS
KFALSIEPKN EALQAYAAQV AHLRNKGLPT IPTTLKIEKA CNPFLRTSST EIRQALGIPD
TANEAEALGV IRQAKDNF
//