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Carboxyethyl-arginine beta-lactam-synthase (EC 6.3.3.4) (Beta-lactam synthetase)

 BLS_STRCL               Reviewed;         513 AA.
P0DJQ7; Q53938; Q9R8E3;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
05-SEP-2012, sequence version 1.
27-SEP-2017, entry version 24.
RecName: Full=Carboxyethyl-arginine beta-lactam-synthase;
EC=6.3.3.4;
AltName: Full=Beta-lactam synthetase;
Name=bls;
Streptomyces clavuligerus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1901;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9689037; DOI=10.1073/pnas.95.16.9082;
Bachmann B.O., Li R., Townsend C.A.;
"Beta-lactam synthetase: a new biosynthetic enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 95:9082-9086(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-513.
PubMed=8529893; DOI=10.1016/0378-1119(95)00560-9;
Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J.,
Arnell J.C., Earl A.J., Lawlor E.J.;
"Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene
cloning and characterization.";
Gene 166:49-55(1995).
[3]
CHARACTERIZATION.
PubMed=10985764; DOI=10.1021/bi000709i;
Bachmann B.O., Townsend C.A.;
"Kinetic mechanism of the beta-lactam synthetase of Streptomyces
clavuligerus.";
Biochemistry 39:11187-11193(2000).
[4]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-507.
PubMed=11473258; DOI=10.1038/90394;
Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.;
"Structure of beta-lactam synthetase reveals how to synthesize
antibiotics instead of asparagine.";
Nat. Struct. Biol. 8:684-689(2001).
[5]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 4-507.
PubMed=12409610; DOI=10.1073/pnas.232361199;
Miller M.T., Bachmann B.O., Townsend C.A., Rosenzweig A.C.;
"The catalytic cycle of beta -lactam synthetase observed by X-ray
crystallographic snapshots.";
Proc. Natl. Acad. Sci. U.S.A. 99:14752-14757(2002).
-!- CATALYTIC ACTIVITY: ATP + L-N(2)-(2-carboxyethyl)arginine = AMP +
diphosphate + deoxyamidinoproclavaminate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis;
clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step
2/8.
-!- SUBUNIT: Homodimer.
-!- SIMILARITY: Belongs to the asparagine synthetase family.
{ECO:0000305}.
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EMBL; AF071051; AAC31901.1; -; Genomic_DNA.
EMBL; X84101; CAA58903.1; -; Genomic_DNA.
PIR; S57668; S57668.
RefSeq; WP_003952510.1; NZ_CP016559.1.
PDB; 1JGT; X-ray; 1.95 A; A/B=1-513.
PDB; 1M1Z; X-ray; 1.95 A; A/B=1-513.
PDB; 1MB9; X-ray; 2.11 A; A/B=1-513.
PDB; 1MBZ; X-ray; 2.47 A; A/B=1-513.
PDB; 1MC1; X-ray; 2.16 A; A/B=1-513.
PDBsum; 1JGT; -.
PDBsum; 1M1Z; -.
PDBsum; 1MB9; -.
PDBsum; 1MBZ; -.
PDBsum; 1MC1; -.
ProteinModelPortal; P0DJQ7; -.
SMR; P0DJQ7; -.
KEGG; ag:AAC31901; -.
KEGG; sclf:BB341_07810; -.
eggNOG; ENOG4105TCH; Bacteria.
eggNOG; COG0367; LUCA.
KO; K12674; -.
BioCyc; MetaCyc:MONOMER-13483; -.
UniPathway; UPA00112; UER00243.
GO; GO:0034027; F:(carboxyethyl)arginine beta-lactam-synthase activity; IEA:UniProtKB-EC.
GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
GO; GO:0033050; P:clavulanic acid biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd01991; Asn_Synthase_B_C; 1.
Gene3D; 3.40.50.620; -; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR001962; Asn_synthase.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF00733; Asn_synthase; 2.
Pfam; PF13537; GATase_7; 1.
SUPFAM; SSF56235; SSF56235; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding;
Nucleotide-binding.
CHAIN 1 513 Carboxyethyl-arginine beta-lactam-
synthase.
/FTId=PRO_0000056939.
METAL 253 253 Magnesium.
METAL 351 351 Magnesium.
STRAND 10 18 {ECO:0000244|PDB:1JGT}.
STRAND 32 36 {ECO:0000244|PDB:1JGT}.
HELIX 42 44 {ECO:0000244|PDB:1JGT}.
STRAND 47 52 {ECO:0000244|PDB:1JGT}.
HELIX 58 61 {ECO:0000244|PDB:1JGT}.
STRAND 62 65 {ECO:0000244|PDB:1JGT}.
STRAND 67 80 {ECO:0000244|PDB:1JGT}.
HELIX 82 87 {ECO:0000244|PDB:1JGT}.
STRAND 89 92 {ECO:0000244|PDB:1MB9}.
HELIX 98 109 {ECO:0000244|PDB:1JGT}.
HELIX 110 115 {ECO:0000244|PDB:1JGT}.
STRAND 119 127 {ECO:0000244|PDB:1JGT}.
STRAND 130 135 {ECO:0000244|PDB:1JGT}.
STRAND 144 148 {ECO:0000244|PDB:1JGT}.
STRAND 151 156 {ECO:0000244|PDB:1JGT}.
HELIX 158 162 {ECO:0000244|PDB:1JGT}.
STRAND 164 166 {ECO:0000244|PDB:1MB9}.
STRAND 175 177 {ECO:0000244|PDB:1JGT}.
STRAND 191 196 {ECO:0000244|PDB:1JGT}.
TURN 197 200 {ECO:0000244|PDB:1JGT}.
STRAND 201 206 {ECO:0000244|PDB:1JGT}.
HELIX 219 237 {ECO:0000244|PDB:1JGT}.
STRAND 240 242 {ECO:0000244|PDB:1MBZ}.
STRAND 245 247 {ECO:0000244|PDB:1JGT}.
HELIX 252 265 {ECO:0000244|PDB:1JGT}.
STRAND 269 274 {ECO:0000244|PDB:1JGT}.
HELIX 281 291 {ECO:0000244|PDB:1JGT}.
STRAND 294 299 {ECO:0000244|PDB:1JGT}.
HELIX 302 306 {ECO:0000244|PDB:1JGT}.
HELIX 309 316 {ECO:0000244|PDB:1JGT}.
HELIX 321 336 {ECO:0000244|PDB:1JGT}.
STRAND 343 345 {ECO:0000244|PDB:1JGT}.
TURN 348 350 {ECO:0000244|PDB:1JGT}.
HELIX 351 354 {ECO:0000244|PDB:1JGT}.
TURN 355 357 {ECO:0000244|PDB:1JGT}.
HELIX 364 376 {ECO:0000244|PDB:1JGT}.
HELIX 386 389 {ECO:0000244|PDB:1JGT}.
TURN 390 392 {ECO:0000244|PDB:1JGT}.
STRAND 394 396 {ECO:0000244|PDB:1JGT}.
HELIX 398 400 {ECO:0000244|PDB:1JGT}.
HELIX 402 410 {ECO:0000244|PDB:1JGT}.
HELIX 413 416 {ECO:0000244|PDB:1JGT}.
STRAND 421 423 {ECO:0000244|PDB:1MBZ}.
HELIX 424 430 {ECO:0000244|PDB:1JGT}.
TURN 431 433 {ECO:0000244|PDB:1JGT}.
HELIX 436 440 {ECO:0000244|PDB:1JGT}.
HELIX 446 449 {ECO:0000244|PDB:1MC1}.
HELIX 455 463 {ECO:0000244|PDB:1JGT}.
TURN 467 469 {ECO:0000244|PDB:1MC1}.
HELIX 470 485 {ECO:0000244|PDB:1JGT}.
TURN 486 488 {ECO:0000244|PDB:1M1Z}.
HELIX 492 494 {ECO:0000244|PDB:1JGT}.
HELIX 497 505 {ECO:0000244|PDB:1JGT}.
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


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