CAS1_STRCL
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 03-AUG-2022, entry version 104.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 / NRRL
RC 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 / NRRL
RC 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 / NRRL
RC 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 / NRRL
RC 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}.
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DR EMBL; L06213; AAA26722.1; -; Genomic_DNA.
DR PIR; A44241; A44241.
DR RefSeq; WP_003961114.1; NZ_CP032052.1.
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; 443255.SCLAV_2925; -.
DR DrugBank; DB02475; Deoxyamidinoproclavaminic acid.
DR DrugBank; DB01985; N-acetyl-L-arginine.
DR PRIDE; Q05581; -.
DR GeneID; 61470965; -.
DR KEGG; ag:AAA26722; -.
DR eggNOG; COG2175; Bacteria.
DR OMA; CLRADHE; -.
DR OrthoDB; 1742732at2; -.
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 Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR014503; Clavaminate_syn-like.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 2.
DR PIRSF; PIRSF019543; Clavaminate_syn; 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
