ID BLS_STRCL Reviewed; 513 AA. AC P0DJQ7; P0DJQ8; Q53938; Q9R8E3; DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 1. DT 27-MAR-2024, entry version 49. DE RecName: Full=Carboxyethyl-arginine beta-lactam-synthase; DE EC=6.3.3.4; DE AltName: Full=Beta-lactam synthetase; GN Name=bls; OS Streptomyces clavuligerus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1901; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9689037; DOI=10.1073/pnas.95.16.9082; RA Bachmann B.O., Li R., Townsend C.A.; RT "Beta-lactam synthetase: a new biosynthetic enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9082-9086(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=10681345; DOI=10.1128/aac.44.3.720-726.2000; RA Jensen S.E., Elder K.J., Aidoo K.A., Paradkar A.S.; RT "Enzymes catalyzing the early steps of clavulanic acid biosynthesis are RT encoded by two sets of paralogous genes in Streptomyces clavuligerus."; RL Antimicrob. Agents Chemother. 44:720-726(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-513. RX PubMed=8529893; DOI=10.1016/0378-1119(95)00560-9; RA Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J., RA Arnell J.C., Earl A.J., Lawlor E.J.; RT "Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning RT and characterization."; RL Gene 166:49-55(1995). RN [4] RP CHARACTERIZATION. RX PubMed=10985764; DOI=10.1021/bi000709i; RA Bachmann B.O., Townsend C.A.; RT "Kinetic mechanism of the beta-lactam synthetase of Streptomyces RT clavuligerus."; RL Biochemistry 39:11187-11193(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-507. RX PubMed=11473258; DOI=10.1038/90394; RA Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.; RT "Structure of beta-lactam synthetase reveals how to synthesize antibiotics RT instead of asparagine."; RL Nat. Struct. Biol. 8:684-689(2001). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 4-507. RX PubMed=12409610; DOI=10.1073/pnas.232361199; RA Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.; RT "The catalytic cycle of beta -lactam synthetase observed by X-ray RT crystallographic snapshots."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14752-14757(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + N(2)-(2-carboxyethyl)-L-arginine = AMP + CC deoxyamidinoproclavaminate + diphosphate + H(+); CC Xref=Rhea:RHEA:23620, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57303, ChEBI:CHEBI:57304, CC ChEBI:CHEBI:456215; EC=6.3.3.4; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate CC from D-glyceraldehyde 3-phosphate and L-arginine: step 2/8. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the asparagine synthetase family. {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; AF071051; AAC31901.1; -; Genomic_DNA. DR EMBL; U87786; AAF86620.1; -; Genomic_DNA. DR EMBL; X84101; CAA58903.1; -; Genomic_DNA. DR PIR; S57668; S57668. DR RefSeq; WP_003952510.1; NZ_WMCC01000013.1. DR PDB; 1JGT; X-ray; 1.95 A; A/B=1-513. DR PDB; 1M1Z; X-ray; 1.95 A; A/B=1-513. DR PDB; 1MB9; X-ray; 2.11 A; A/B=1-513. DR PDB; 1MBZ; X-ray; 2.47 A; A/B=1-513. DR PDB; 1MC1; X-ray; 2.16 A; A/B=1-513. DR PDBsum; 1JGT; -. DR PDBsum; 1M1Z; -. DR PDBsum; 1MB9; -. DR PDBsum; 1MBZ; -. DR PDBsum; 1MC1; -. DR AlphaFoldDB; P0DJQ7; -. DR SMR; P0DJQ7; -. DR STRING; 1901.BB341_07810; -. DR GeneID; 61469724; -. DR KEGG; ag:AAC31901; -. DR eggNOG; COG0367; Bacteria. DR OrthoDB; 9763290at2; -. DR BioCyc; MetaCyc:MONOMER-13483; -. DR BRENDA; 6.3.3.4; 5988. DR UniPathway; UPA00112; UER00243. DR GO; GO:0034027; F:(carboxyethyl)arginine beta-lactam-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro. DR GO; GO:0033050; P:clavulanic acid biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01991; Asn_Synthase_B_C; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR InterPro; IPR001962; Asn_synthase. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR11772; ASPARAGINE SYNTHETASE; 1. DR PANTHER; PTHR11772:SF2; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1. DR Pfam; PF00733; Asn_synthase; 2. DR Pfam; PF13537; GATase_7; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding. FT CHAIN 1..513 FT /note="Carboxyethyl-arginine beta-lactam-synthase" FT /id="PRO_0000056939" FT BINDING 253 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT STRAND 10..18 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 67..80 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 82..87 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:1MB9" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 119..127 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 158..162 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:1MB9" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 191..196 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 219..237 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1MBZ" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 252..265 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 281..291 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 302..306 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 309..316 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 321..336 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 351..354 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 364..376 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 390..392 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 402..410 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 413..416 FT /evidence="ECO:0007829|PDB:1JGT" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:1MBZ" FT HELIX 424..430 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 431..433 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 436..440 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 446..449 FT /evidence="ECO:0007829|PDB:1MC1" FT HELIX 455..463 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 467..469 FT /evidence="ECO:0007829|PDB:1MC1" FT HELIX 470..485 FT /evidence="ECO:0007829|PDB:1JGT" FT TURN 486..488 FT /evidence="ECO:0007829|PDB:1M1Z" FT HELIX 492..494 FT /evidence="ECO:0007829|PDB:1JGT" FT HELIX 497..505 FT /evidence="ECO:0007829|PDB:1JGT" SQ SEQUENCE 513 AA; 54530 MW; EC2F460A77EB65CE CRC64; MGAPVLPAAF GFLASARTGG GRAPGPVFAT RGSHTDIDTP QGERSLAATL VHAPSVAPDR AVARSLTGAP TTAVLAGEIY NRDELLSVLP AGPAPEGDAE LVLRLLERYD LHAFRLVNGR FATVVRTGDR VLLATDHAGS VPLYTCVAPG EVRASTEAKA LAAHRDPKGF PLADARRVAG LTGVYQVPAG AVMDIDLGSG TAVTHRTWTP GLSRRILPEG EAVAAVRAAL EKAVAQRVTP GDTPLVVLSG GIDSSGVAAC AHRAAGELDT VSMGTDTSNE FREARAVVDH LRTRHREITI PTTELLAQLP YAVWASESVD PDIIEYLLPL TALYRALDGP ERRILTGYGA DIPLGGMHRE DRLPALDTVL AHDMATFDGL NEMSPVLSTL AGHWTTHPYW DREVLDLLVS LEAGLKRRHG RDKWVLRAAM ADALPAETVN RPKLGVHEGS GTTSSFSRLL LDHGVAEDRV HEAKRQVVRE LFDLTVGGGR HPSEVDTDDV VRSVADRTAR GAA //