Q05581 (CAS1_STRC2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Clavaminate synthase 1
EC=1.14.11.21

Alternative name(s):
Clavaminic acid synthase 1
Short name=CAS1
Short name=CS1

Gene names

Name:

cs1

Organism

Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)

Taxonomic identifier

443255 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces clavuligerus

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2. Proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O. Dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O.
Cofactor	Binds 1 Fe2+ ion per subunit.
Pathway	Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 3/8. Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 5/8. Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate from D-glyceraldehyde 3-phosphate and L-arginine: step 6/8.
Sequence similarities	Belongs to the clavaminate synthase family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW clavulanic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	clavaminate synthase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 324

323

Clavaminate synthase 1

PRO_0000089322

Sites

Metal binding

144

1

Iron

Metal binding

146

1

Iron

Metal binding

279

1

Iron

Binding site

293

1

2-oxoglutarate By similarity

Secondary structure

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324

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

7 – 9

3

Helix

10 – 18

9

Helix

24 – 27

4

Helix

28 – 39

12

Helix

44 – 56

13

Beta strand

61 – 67

7

Helix

73 – 75

3

Beta strand

82 – 84

3

Helix

93 – 105

13

Beta strand

107 – 111

5

Helix

115 – 117

3

Beta strand

119 – 123

5

Beta strand

137 – 139

3

Beta strand

141 – 144

4

Turn

146 – 149

4

Beta strand

155 – 163

9

Beta strand

172 – 176

5

Helix

177 – 180

4

Helix

181 – 183

3

Helix

186 – 192

7

Beta strand

197 – 199

3

Helix

203 – 205

3

Helix

212 – 214

3

Beta strand

215 – 218

4

Beta strand

220 – 223

4

Turn

234 – 236

3

Helix

242 – 257

16

Beta strand

260 – 262

3

Beta strand

269 – 273

5

Turn

274 – 276

3

Beta strand

277 – 281

5

Beta strand

294 – 301

8

Helix

304 – 306

3

Beta strand

316 – 318

3

Sequences

	Sequence		Length	Mass (Da)
	Q05581 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F5C251134CA4933E	FASTA	324	35,370
	10 20 30 40 50 60 MTSVDCTAYG PELRALAARL PRTPRADLYA FLDAAHTAAA SLPGALATAL DTFNAEGSED 70 80 90 100 110 120 GHLLLRGLPV EADADLPTTP SSTPAPEDRS LLTMEAMLGL VGRRLGLHTG YRELRSGTVY 130 140 150 160 170 180 HDVYPSPGAH HLSSETSETL LEFHTEMAYH RLQPNYVMLA CSRADHERTA ATLVASVRKA 190 200 210 220 230 240 LPLLDERTRA RLLDRRMPCC VDVAFRGGVD DPGAIAQVKP LYGDADDPFL GYDRELLAPE 250 260 270 280 290 300 DPADKEAVAA LSKALDEVTE AVYLEPGDLL IVDNFRTTHA RTPFSPRWDG KDRWLHRVYI 310 320 RTDRNGQLSG GERAGDVVAF TPRG

References

[1]	"Two isozymes of clavaminate synthase central to clavulanic acid formation: cloning and sequencing of both genes from Streptomyces clavuligerus." Marsh E.N., Chang M.D.-T., Townsend C.A. Biochemistry 31:12648-12657(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21. Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[2]	"Expression and purification of two isozymes of clavaminate synthase and initial characterization of the iron binding site. General error analysis in polymerase chain reaction amplification." Busby R.W., Chang M.D.-T., Busby R.C., Wimp J., Townsend C.A. J. Biol. Chem. 270:4262-4269(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[3]	"Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase." Zhang Z., Ren J.-S., Stammers D.K., Baldwin J.E., Harlos K., Schofield C.J. Nat. Struct. Biol. 7:127-133(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS). Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[4]	"Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements." Zhang Z., Ren J.-S., Harlos K., McKinnon C.H., Clifton I.J., Schofield C.J. FEBS Lett. 517:7-12(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS). Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06213 Genomic DNA. Translation: AAA26722.1.

PIR

A44241.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DRT	X-ray	2.10	A	1-324	[»]
1DRY	X-ray	1.40	A	1-324	[»]
1DS0	X-ray	1.63	A	1-324	[»]
1DS1	X-ray	1.08	A	1-324	[»]
1GVG	X-ray	1.54	A	1-324	[»]

ProteinModelPortal

Q05581.

SMR

Q05581. Positions 2-324.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00112; UER00244.
UPA00112; UER00246.
UPA00112; UER00247.

Family and domain databases

InterPro

IPR014503. Clavaminate_syn.
IPR003819. Taurine_dOase.
[Graphical view]

Pfam

PF02668. TauD. 2 hits.
[Graphical view]

PIRSF

PIRSF019543. Clavaminate_syn. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q05581.

Entry information

Entry name

CAS1_STRC2

Accession

Primary (citable) accession number: Q05581

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program