P00590 (CUTI1_FUSSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cutinase 1
EC=3.1.1.74

Alternative name(s):
Cutin hydrolase 1

Gene names

Name:	CUT1
Synonyms:	CUTA

Organism

Fusarium solani subsp. pisi (Nectria haematococca)

Taxonomic identifier

70791 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Nectria › Nectria haematococca complex › Nectria haematococca

Protein attributes

Sequence length	230 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)

Function	Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.
Catalytic activity	Cutin + H2O = cutin monomers.
Subcellular location	Secreted.
Induction	By contact with cutin.
Post-translational modification	The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid. Ref.3
Sequence similarities	Belongs to the cutinase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW cutinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Chain

32 – 230

199

Cutinase 1

PRO_0000006440

Sites

Active site

136

1

Active site

191

1

Active site

204

1

Amino acid modifications

Modified residue

32

1

N-D-glucuronoyl glycine Ref.3

Disulfide bond

47 ↔ 194

Disulfide bond

125 ↔ 187

Experimental info

Sequence conflict

48

1

R → A in AAA33335. Ref.2

Sequence conflict

94

1

R → A in AAA33335. Ref.2

Secondary structure

1

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230

Helix Strand Turn

Details...

Turn

38 – 41

4

Helix

44 – 46

3

Beta strand

49 – 55

7

Turn

62 – 67

6

Helix

68 – 79

12

Turn

81 – 83

3

Beta strand

84 – 88

5

Helix

97 – 101

5

Helix

108 – 124

17

Beta strand

129 – 135

7

Helix

137 – 148

12

Helix

151 – 154

4

Beta strand

157 – 164

8

Turn

166 – 173

8

Helix

180 – 182

3

Beta strand

183 – 186

4

Helix

192 – 195

4

Helix

202 – 205

4

Helix

208 – 212

5

Helix

214 – 227

14

Sequences

	Sequence		Length	Mass (Da)
	P00590 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 7253ACAA657AD1AB	FASTA	230	23,982
	10 20 30 40 50 60 MKFFALTTLL AATASALPTS NPAQELEARQ LGRTTRDDLI NGNSASCRDV IFIYARGSTE 70 80 90 100 110 120 TGNLGTLGPS IASNLESAFG KDGVWIQGVG GAYRATLGDN ALPRGTSSAA IREMLGLFQQ 130 140 150 160 170 180 ANTKCPDATL IAGGYSQGAA LAAASIEDLD SAIRDKIAGT VLFGYTKNLQ NRGRIPNYPA 190 200 210 220 230 DRTKVFCNTG DLVCTGSLIV AAPHLAYGPD ARGPAPEFLI EKVRAVRGSA

References

[1]	"Cloning and structure determination of cDNA for cutinase, an enzyme involved in fungal penetration of plants." Soliday C.L., Flurkey W.H., Okita T.W., Kolattukudy P.E. Proc. Natl. Acad. Sci. U.S.A. 81:3939-3943(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 57-94; 113-142 AND 183-192. Strain: T-8.
[2]	"Structure of the cutinase gene and detection of promoter activity in the 5'-flanking region by fungal transformation." Soliday C.L., Dickman M.B., Kolattukudy P.E. J. Bacteriol. 171:1942-1951(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus." Lin T.-S., Kolattukudy P.E. Eur. J. Biochem. 106:341-351(1980) [PubMed] [Europe PMC] [Abstract] Cited for: GLUCURONIC-ACID BINDING AT GLY-32, GLYCOSYLATION.
[4]	"Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent." Martinez C., de Geus P., Lauwereys M., Matthyssens G., Cambillau C. Nature 356:615-618(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[5]	"Cutinase, a lipolytic enzyme with a preformed oxyanion hole." Martinez C., Nicolas A., van Tilbeurgh H., Egloff M.-P., Cudrey C., Verger R., Cambillau C. Biochemistry 33:83-89(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]	"Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis." Longhi S., Czjzek M., Lamzin V., Nicolas A., Cambillau C. J. Mol. Biol. 268:779-799(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 17-230.
[7]	Nicolas A., Martinez C., Cambillau C. Submitted (MAR-1997) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 33-230.
[8]	"1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution." Prompers J.J., Groenewegen A., van Schaik R.C., Pepermans H.A.M., Hilbers C.W. Protein Sci. 6:2375-2384(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02640 mRNA. Translation: AAA33334.1.
M29759 Genomic DNA. Translation: AAA33335.1.

PIR

UVFUS. A32836.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AGY	X-ray	1.15	A	31-230	[»]
1CEX	X-ray	1.00	A	17-230	[»]
1CUA	X-ray	1.80	A	17-230	[»]
1CUB	X-ray	1.75	A	17-230	[»]
1CUC	X-ray	1.75	A	17-230	[»]
1CUD	X-ray	2.70	A/B/C	17-230	[»]
1CUE	X-ray	2.10	A	33-229	[»]
1CUF	X-ray	1.75	A	17-230	[»]
1CUG	X-ray	1.75	A	17-230	[»]
1CUH	X-ray	1.75	A	17-230	[»]
1CUI	X-ray	2.50	A	17-230	[»]
1CUJ	X-ray	1.60	A	17-230	[»]
1CUS	X-ray	1.25	A	31-230	[»]
1CUU	X-ray	1.69	A	17-230	[»]
1CUV	X-ray	2.01	A	17-230	[»]
1CUW	X-ray	2.70	A/B	17-230	[»]
1CUX	X-ray	1.75	A	17-230	[»]
1CUY	X-ray	1.69	A	17-230	[»]
1CUZ	X-ray	2.10	A	17-230	[»]
1FFA	X-ray	1.69	A	17-230	[»]
1FFB	X-ray	1.75	A	17-230	[»]
1FFC	X-ray	1.75	A	17-230	[»]
1FFD	X-ray	1.69	A	17-230	[»]
1FFE	X-ray	1.69	A	17-230	[»]
1OXM	X-ray	2.30	A/B	17-230	[»]
1XZA	X-ray	1.80	A	17-230	[»]
1XZB	X-ray	1.75	A	17-230	[»]
1XZC	X-ray	1.75	A	17-230	[»]
1XZD	X-ray	2.70	A	17-228	[»]
1XZE	X-ray	1.75	A	17-230	[»]
1XZF	X-ray	1.69	A	17-230	[»]
1XZG	X-ray	1.69	A	17-230	[»]
1XZH	X-ray	1.69	A	17-230	[»]
1XZI	X-ray	1.69	A	17-230	[»]
1XZJ	X-ray	1.69	A	17-230	[»]
1XZK	X-ray	2.01	A/B	17-230	[»]
1XZL	X-ray	1.69	A	17-230	[»]
1XZM	X-ray	1.75	A	17-230	[»]
2CUT	X-ray	1.90	A	31-228	[»]
3EF3	X-ray	1.50	A	17-230	[»]
3ESA	X-ray	2.00	A/B	17-230	[»]
3ESB	X-ray	2.30	A	17-230	[»]
3ESC	X-ray	1.20	A	17-230	[»]
3ESD	X-ray	1.22	A	17-230	[»]
3QPA	X-ray	0.85	A	32-228	[»]
3QPC	X-ray	0.98	A	32-228	[»]

ProteinModelPortal

P00590.

SMR

P00590. Positions 33-229.

ModBase

Search...

PTM databases

GlycoSuiteDB

P00590.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.1.1.74. 9402.

Family and domain databases

InterPro

IPR000675. Cutinase.
IPR011150. Cutinase_monf.
[Graphical view]

Pfam

PF01083. Cutinase. 1 hit.
[Graphical view]

PRINTS

PR00129. CUTINASE.

PROSITE

PS00155. CUTINASE_1. 1 hit.
PS00931. CUTINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00590.

Entry information

Entry name

CUTI1_FUSSO

Accession

Primary (citable) accession number: P00590

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program