BLS_STRCL
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 03-AUG-2022, entry version 40.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 / NRRL
RC 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}.
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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_CP032052.1.
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; 443255.SCLAV_4196; -.
DR PRIDE; P0DJQ7; -.
DR GeneID; 61469724; -.
DR KEGG; ag:AAC31901; -.
DR eggNOG; COG0367; Bacteria.
DR OMA; RIAARHF; -.
DR OrthoDB; 610569at2; -.
DR BioCyc; MetaCyc:MON-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; 3.40.50.620; -; 1.
DR Gene3D; 3.60.20.10; -; 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 Pfam; PF00733; Asn_synthase; 2.
DR Pfam; PF13537; GATase_7; 1.
DR SUPFAM; SSF56235; SSF56235; 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
