Y2304_BURP1
ID Y2304_BURP1 Reviewed; 294 AA.
AC Q3JRV4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Probable metallo-hydrolase BURPS1710b_2304;
DE EC=3.-.-.-;
GN OrderedLocusNames=BURPS1710b_2304;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP LACK OF BETA-LACTAMASE ACTIVITY, AND METAL-BINDING.
RC STRAIN=1710b;
RA Phan I.;
RL Submitted (MAY-2012) to UniProtKB.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RC STRAIN=1710b;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of a hypothetical metallo-beta-lactamase from
RT Burkholderia pseudomallei.";
RL Submitted (MAY-2012) to the PDB data bank.
CC -!- FUNCTION: Probable hydrolase. Does not have beta-lactamase activity.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- MISCELLANEOUS: The heavy atoms seen in the catalytic site in the
CC crystallographic structure were modeled as calcium ions due to the
CC electron density. However, it is possible that these are larger metals
CC such as zinc or iron that have low occupancy in the catalytic site.
CC Indeed, zinc and iron ions are both observed in metallo-beta-lactamase
CC superfamily members.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; CP000124; ABA48988.1; -; Genomic_DNA.
DR RefSeq; WP_004521366.1; NC_007434.1.
DR PDB; 4EFZ; X-ray; 1.60 A; A/B=1-294.
DR PDBsum; 4EFZ; -.
DR AlphaFoldDB; Q3JRV4; -.
DR SMR; Q3JRV4; -.
DR EnsemblBacteria; ABA48988; ABA48988; BURPS1710b_2304.
DR GeneID; 56529286; -.
DR KEGG; bpm:BURPS1710b_2304; -.
DR HOGENOM; CLU_030571_6_1_4; -.
DR OMA; LYLCHDY; -.
DR Proteomes; UP000002700; Chromosome I.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
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 Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding.
FT CHAIN 1..294
FT /note="Probable metallo-hydrolase BURPS1710b_2304"
FT /id="PRO_0000425277"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4EFZ"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:4EFZ"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:4EFZ"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:4EFZ"
SQ SEQUENCE 294 AA; 32091 MW; 44E865F481117D97 CRC64;
MTVEGFFDPA TCTISYLLFD SGSGECALID SVLDYDPKSG RTRTASADQL IARVAALGAR
VRWLLETHVH ADHLSAAPYL KTRVGGEIAI GRHVTRVQDV FGKLFNAGPA FAHDGSQFDR
LLDDGDTLAL GALSIRAMHT PGHTPACMTY VVTEAHAAHD ARDAAAFVGD TLFMPDYGTA
RCDFPGGDAR SLYRSIRKVL SLPPATRLYM CHDYQPNGRA IQYASTVADE LRENVHIREG
VTEDDFVAMR TARDATLDMP VLMLPSVQVN MRAGRLPEPE DNGVRYLKIP LDAI
