ID BLO10_PSEAI Reviewed; 266 AA. AC P14489; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 24-JAN-2024, entry version 143. DE RecName: Full=Beta-lactamase OXA-10; DE EC=3.5.2.6; DE AltName: Full=Beta-lactamase PSE-2; DE Flags: Precursor; GN Name=bla; Synonyms=oxa10, pse2; OS Pseudomonas aeruginosa. OG Plasmid pMON234. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TRANSPOSON=Tn1404; RX PubMed=3126705; DOI=10.1128/aac.32.1.134; RA Huovinen P., Huovinen S., Jacoby G.A.; RT "Sequence of PSE-2 beta-lactamase."; RL Antimicrob. Agents Chemother. 32:134-136(1988). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 21-266, AND CARBOXYLATION AT RP LYS-70. RX PubMed=11188693; DOI=10.1016/s0969-2126(00)00534-7; RA Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S., RA Mobashery S., Samama J.-P.; RT "Insights into class D beta-lactamases are revealed by the crystal RT structure of the OXA10 enzyme from Pseudomonas aeruginosa."; RL Structure 8:1289-1298(2000). CC -!- FUNCTION: Hydrolyzes both carbenicillin and oxacillin. CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid; CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, CC ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10103}; CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U37105; AAB60534.1; -; Genomic_DNA. DR EMBL; J03427; AAA25648.1; -; Genomic_DNA. DR PIR; S06462; S06462. DR RefSeq; WP_000846390.1; NZ_WXZW01000004.1. DR PDB; 1E3U; X-ray; 1.66 A; A/B/C/D=21-266. DR PDB; 1E4D; X-ray; 1.80 A; A/B/C/D=21-266. DR PDB; 1EWZ; X-ray; 2.40 A; A/B/C/D=21-266. DR PDB; 1FOF; X-ray; 2.00 A; A/B=20-265. DR PDB; 1K4E; X-ray; 2.00 A; A/B=20-266. DR PDB; 1K4F; X-ray; 1.60 A; A/B=20-266. DR PDB; 1K54; X-ray; 1.70 A; A/B/C/D=21-266. DR PDB; 1K55; X-ray; 1.39 A; A/B/C/D=21-266. DR PDB; 1K56; X-ray; 1.70 A; A/B/C/D=21-266. DR PDB; 1K57; X-ray; 1.90 A; A/B/C/D=21-266. DR PDB; 1K6R; X-ray; 2.30 A; A/B=20-266. DR PDB; 1K6S; X-ray; 2.03 A; A/B=20-266. DR PDB; 2HP5; X-ray; 2.70 A; A/B/C/D=20-266. DR PDB; 2HP6; X-ray; 2.20 A; A/B=20-266. DR PDB; 2HP9; X-ray; 2.50 A; A/B=20-266. DR PDB; 2HPB; X-ray; 2.05 A; A/B=20-266. DR PDB; 2RL3; X-ray; 1.90 A; A/B=20-266. DR PDB; 2WGI; X-ray; 2.85 A; A/B=21-266. DR PDB; 2WGV; X-ray; 1.80 A; A/B=20-266. DR PDB; 2WGW; X-ray; 1.80 A; A/B=20-266. DR PDB; 2WKH; X-ray; 1.79 A; A/B=20-266. DR PDB; 2WKI; X-ray; 2.10 A; A/B=20-266. DR PDB; 2X01; X-ray; 1.90 A; A/B=20-266. DR PDB; 2X02; X-ray; 1.35 A; A/B=20-266. DR PDB; 3LCE; X-ray; 2.00 A; A/B/C/D=21-266. DR PDB; 4S2O; X-ray; 1.70 A; A/B=20-265. DR PDB; 4WZ5; X-ray; 1.60 A; A/B/C/D=20-266. DR PDB; 5FQ9; X-ray; 1.50 A; A/B=20-266. DR PDB; 5MMY; X-ray; 1.88 A; A/B=20-264. DR PDB; 5MNU; X-ray; 1.56 A; A/B=20-265. DR PDB; 5MOX; X-ray; 1.41 A; A/B=20-265. DR PDB; 5MOZ; X-ray; 1.34 A; A/B=20-265. DR PDB; 6RTN; X-ray; 2.17 A; A/B=20-265. DR PDB; 7B3R; X-ray; 1.83 A; A/B=20-265. DR PDB; 7B3S; X-ray; 1.85 A; A/B=20-265. DR PDB; 7B3U; X-ray; 1.60 A; A/B=20-265. DR PDB; 7L5R; X-ray; 1.65 A; A/B=21-266. DR PDB; 7L5T; X-ray; 1.88 A; A/B=21-266. DR PDB; 7L5V; X-ray; 1.30 A; A/B=19-266. DR PDBsum; 1E3U; -. DR PDBsum; 1E4D; -. DR PDBsum; 1EWZ; -. DR PDBsum; 1FOF; -. DR PDBsum; 1K4E; -. DR PDBsum; 1K4F; -. DR PDBsum; 1K54; -. DR PDBsum; 1K55; -. DR PDBsum; 1K56; -. DR PDBsum; 1K57; -. DR PDBsum; 1K6R; -. DR PDBsum; 1K6S; -. DR PDBsum; 2HP5; -. DR PDBsum; 2HP6; -. DR PDBsum; 2HP9; -. DR PDBsum; 2HPB; -. DR PDBsum; 2RL3; -. DR PDBsum; 2WGI; -. DR PDBsum; 2WGV; -. DR PDBsum; 2WGW; -. DR PDBsum; 2WKH; -. DR PDBsum; 2WKI; -. DR PDBsum; 2X01; -. DR PDBsum; 2X02; -. DR PDBsum; 3LCE; -. DR PDBsum; 4S2O; -. DR PDBsum; 4WZ5; -. DR PDBsum; 5FQ9; -. DR PDBsum; 5MMY; -. DR PDBsum; 5MNU; -. DR PDBsum; 5MOX; -. DR PDBsum; 5MOZ; -. DR PDBsum; 6RTN; -. DR PDBsum; 7B3R; -. DR PDBsum; 7B3S; -. DR PDBsum; 7B3U; -. DR PDBsum; 7L5R; -. DR PDBsum; 7L5T; -. DR PDBsum; 7L5V; -. DR AlphaFoldDB; P14489; -. DR SMR; P14489; -. DR BindingDB; P14489; -. DR ChEMBL; CHEMBL5482; -. DR DrugBank; DB02122; 4-iodo-acetamido phenylboronic acid. DR DrugBank; DB04342; 7-((Carboxy(4-Hydroxyphenyl)Acetyl)Amino)-7-Methoxy-(3-((1-Methyl-1h-Tetrazol-5-Yl)Thio)Methyl)-8-Oxo-5-Oxa-1-Azabicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR DrugBank; DB00760; Meropenem. DR GeneID; 84239014; -. DR KEGG; ag:AAB60534; -. DR BRENDA; 3.5.2.6; 5087. DR EvolutionaryTrace; P14489; -. DR PRO; PR:P14489; -. DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR002137; Beta-lactam_class-D_AS. DR InterPro; IPR001460; PCN-bd_Tpept. DR PANTHER; PTHR30627:SF6; BETA-LACTAMASE YBXI-RELATED; 1. DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR PROSITE; PS00337; BETA_LACTAMASE_D; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid; KW Signal; Transposable element. FT SIGNAL 1..20 FT CHAIN 21..266 FT /note="Beta-lactamase OXA-10" FT /id="PRO_0000017030" FT ACT_SITE 67 FT /note="Acyl-ester intermediate" FT BINDING 205..207 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 70 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:11188693" FT DISULFID 44..51 FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 29..34 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 39..47 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1E3U" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 108..113 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 117..127 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:7L5V" FT TURN 150..155 FT /evidence="ECO:0007829|PDB:5MOZ" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:5MOZ" FT HELIX 163..174 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 182..191 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 200..208 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:7B3S" FT STRAND 214..228 FT /evidence="ECO:0007829|PDB:7L5V" FT STRAND 231..243 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 244..248 FT /evidence="ECO:0007829|PDB:7L5V" FT HELIX 249..260 FT /evidence="ECO:0007829|PDB:7L5V" SQ SEQUENCE 266 AA; 29507 MW; 9ABFF429D028F240 CRC64; MKTFAAYVII ACLSSTALAG SITENTSWNK EFSAEAVNGV FVLCKSSSKS CATNDLARAS KEYLPASTFK IPNAIIGLET GVIKNEHQVF KWDGKPRAMK QWERDLTLRG AIQVSAVPVF QQIAREVGEV RMQKYLKKFS YGNQNISGGI DKFWLEGQLR ISAVNQVEFL ESLYLNKLSA SKENQLIVKE ALVTEAAPEY LVHSKTGFSG VGTESNPGVA WWVGWVEKET EVYFFAFNMD IDNESKLPLR KSIPTKIMES EGIIGG //