ID CAS1_STRCL Reviewed; 324 AA. AC Q05581; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 110. DE RecName: Full=Clavaminate synthase 1; DE EC=1.14.11.21; DE AltName: Full=Clavaminic acid synthase 1; DE Short=CAS1; DE Short=CS1; GN Name=cs1; OS Streptomyces clavuligerus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1901; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=1472501; DOI=10.1021/bi00165a015; RA Marsh E.N., Chang M.D.-T., Townsend C.A.; RT "Two isozymes of clavaminate synthase central to clavulanic acid formation: RT cloning and sequencing of both genes from Streptomyces clavuligerus."; RL Biochemistry 31:12648-12657(1992). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=7876185; DOI=10.1074/jbc.270.9.4262; RA Busby R.W., Chang M.D.-T., Busby R.C., Wimp J., Townsend C.A.; RT "Expression and purification of two isozymes of clavaminate synthase and RT initial characterization of the iron binding site. General error analysis RT in polymerase chain reaction amplification."; RL J. Biol. Chem. 270:4262-4269(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS). RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=10655615; DOI=10.1038/72398; RA Zhang Z., Ren J.-S., Stammers D.K., Baldwin J.E., Harlos K., RA Schofield C.J.; RT "Structural origins of the selectivity of the trifunctional oxygenase RT clavaminic acid synthase."; RL Nat. Struct. Biol. 7:127-133(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS). RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=12062399; DOI=10.1016/s0014-5793(02)02520-6; RA Zhang Z., Ren J.-S., Harlos K., McKinnon C.H., Clifton I.J., RA Schofield C.J.; RT "Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate- RT substrate-NO complex: evidence for metal centered rearrangements."; RL FEBS Lett. 517:7-12(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + deoxyamidinoproclavaminate + O2 = CC amidinoproclavaminate + CO2 + succinate; Xref=Rhea:RHEA:20021, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57303, ChEBI:CHEBI:58647; CC EC=1.14.11.21; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + O2 + proclavaminate = CO2 + CC dihydroclavaminate + H2O + succinate; Xref=Rhea:RHEA:12773, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57301, CC ChEBI:CHEBI:57302; EC=1.14.11.21; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + dihydroclavaminate + O2 = clavaminate + CO2 + CC H2O + succinate; Xref=Rhea:RHEA:19785, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57300, ChEBI:CHEBI:57301; CC EC=1.14.11.21; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 1 Fe(2+) ion per subunit.; CC -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate CC from D-glyceraldehyde 3-phosphate and L-arginine: step 3/8. CC -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate CC from D-glyceraldehyde 3-phosphate and L-arginine: step 5/8. CC -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate CC from D-glyceraldehyde 3-phosphate and L-arginine: step 6/8. CC -!- SIMILARITY: Belongs to the clavaminate synthase 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; L06213; AAA26722.1; -; Genomic_DNA. DR PIR; A44241; A44241. DR RefSeq; WP_003961114.1; NZ_JADANO010000002.1. DR PDB; 1DRT; X-ray; 2.10 A; A=1-324. DR PDB; 1DRY; X-ray; 1.40 A; A=1-324. DR PDB; 1DS0; X-ray; 1.63 A; A=1-324. DR PDB; 1DS1; X-ray; 1.08 A; A=1-324. DR PDB; 1GVG; X-ray; 1.54 A; A=1-324. DR PDBsum; 1DRT; -. DR PDBsum; 1DRY; -. DR PDBsum; 1DS0; -. DR PDBsum; 1DS1; -. DR PDBsum; 1GVG; -. DR AlphaFoldDB; Q05581; -. DR SMR; Q05581; -. DR STRING; 1901.BB341_13950; -. DR DrugBank; DB02475; Deoxyamidinoproclavaminic acid. DR DrugBank; DB01985; N-acetyl-L-arginine. DR GeneID; 61470965; -. DR KEGG; ag:AAA26722; -. DR eggNOG; COG2175; Bacteria. DR OrthoDB; 3872700at2; -. DR BRENDA; 1.14.11.21; 5988. DR UniPathway; UPA00112; UER00244. DR UniPathway; UPA00112; UER00246. DR UniPathway; UPA00112; UER00247. DR EvolutionaryTrace; Q05581; -. DR GO; GO:0033758; F:clavaminate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0033050; P:clavulanic acid biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00250; CAS_like; 1. DR Gene3D; 3.60.130.10; Clavaminate synthase-like; 1. DR InterPro; IPR014503; Clavaminate_syn-like. DR InterPro; IPR042098; TauD-like_sf. DR InterPro; IPR003819; TauD/TfdA-like. DR PANTHER; PTHR10696; GAMMA-BUTYROBETAINE HYDROXYLASE-RELATED; 1. DR PANTHER; PTHR10696:SF21; TAUD_TFDA-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF02668; TauD; 1. DR PIRSF; PIRSF019543; Clavaminate_syn; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic biosynthesis; Direct protein sequencing; Iron; KW Metal-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1472501" FT CHAIN 2..324 FT /note="Clavaminate synthase 1" FT /id="PRO_0000089322" FT BINDING 144 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 146 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 279 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 293 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000250" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 10..18 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 28..39 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 44..56 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 93..105 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1GVG" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:1DS1" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 155..163 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 186..192 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:1DS1" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 242..257 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:1DS1" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 294..301 FT /evidence="ECO:0007829|PDB:1DS1" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:1DS1" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:1DS1" SQ SEQUENCE 324 AA; 35370 MW; F5C251134CA4933E CRC64; MTSVDCTAYG PELRALAARL PRTPRADLYA FLDAAHTAAA SLPGALATAL DTFNAEGSED GHLLLRGLPV EADADLPTTP SSTPAPEDRS LLTMEAMLGL VGRRLGLHTG YRELRSGTVY HDVYPSPGAH HLSSETSETL LEFHTEMAYH RLQPNYVMLA CSRADHERTA ATLVASVRKA LPLLDERTRA RLLDRRMPCC VDVAFRGGVD DPGAIAQVKP LYGDADDPFL GYDRELLAPE DPADKEAVAA LSKALDEVTE AVYLEPGDLL IVDNFRTTHA RTPFSPRWDG KDRWLHRVYI RTDRNGQLSG GERAGDVVAF TPRG //