Q00017 (RHA1_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rhamnogalacturonan acetylesterase
Short name=RGAE
EC=3.1.1.86

Gene names

Name:

rha1

Organism

Aspergillus aculeatus

Taxonomic identifier

5053 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	250 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	Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B). Ref.1
Catalytic activity	Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I. Ref.1
Post-translational modification	Carbohydrate at Asn-199 is composed of GlcNAc and Man.
Sequence similarities	Belongs to the 'GDSL' lipolytic enzyme family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.1

Chain

18 – 250

233

Rhamnogalacturonan acetylesterase

PRO_0000017852

Sites

Active site

26

1

Nucleophile Probable

Active site

209

1

Active site

212

1

Amino acid modifications

Glycosylation

121

1

N-linked (GlcNAc...) Ref.3 Ref.4 Ref.5

Glycosylation

199

1

N-linked (GlcNAc...) (high mannose) Ref.3 Ref.4 Ref.5

Disulfide bond

105 ↔ 113

Ref.5

Disulfide bond

231 ↔ 249

Ref.5

Secondary structure

1

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250

Helix Strand Turn

Details...

Beta strand

19 – 23

5

Turn

26 – 28

3

Turn

30 – 33

4

Helix

40 – 43

4

Helix

45 – 47

3

Beta strand

48 – 54

7

Helix

62 – 67

6

Helix

70 – 77

8

Beta strand

83 – 86

4

Helix

96 – 98

3

Beta strand

105 – 110

6

Beta strand

112 – 117

6

Beta strand

120 – 126

7

Helix

127 – 140

14

Beta strand

144 – 148

5

Turn

155 – 158

4

Helix

167 – 179

13

Beta strand

182 – 184

3

Helix

186 – 197

12

Helix

199 – 204

6

Beta strand

207 – 211

5

Helix

215 – 232

18

Helix

235 – 239

5

Sequences

	Sequence		Length	Mass (Da)
	Q00017 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C30676A3A876A38B	FASTA	250	26,351
	10 20 30 40 50 60 MKTAALAPLF FLPSALATTV YLAGDSTMAK NGGGSGTNGW GEYLASYLSA TVVNDAVAGR 70 80 90 100 110 120 SARSYTREGR FENIADVVTA GDYVIVEFGH NDGGSLSTDN GRTDCSGTGA EVCYSVYDGV 130 140 150 160 170 180 NETILTFPAY LENAAKLFTA KGAKVILSSQ TPNNPWETGT FVNSPTRFVE YAELAAEVAG 190 200 210 220 230 240 VEYVDHWSYV DSIYETLGNA TVNSYFPIDH THTSPAGAEV VAEAFLKAVV CTGTSLKSVL 250 TTTSFEGTCL

References

[1]	"Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Synergism between rhamnogalacturonan degrading enzymes." Kauppinen S., Christgau S., Kofod L.V., Halkier T., Doerreich K., Dalboege H. J. Biol. Chem. 270:27172-27178(1995) [PubMed: 7592973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-45, FUNCTION, CATALYTIC ACTIVITY. Strain: KSM 510.
[2]	"Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus." Moelgaard A., Petersen J.F.W., Kauppinen S., Dalboege H., Johnsen A.H., Navarro Poulsen J.-C., Larsen S. Acta Crystallogr. D 54:1026-1029(1998) [PubMed: 9757128] [Abstract] Cited for: CRYSTALLIZATION.
[3]	"Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases." Moelgaard A., Kauppinen S., Larsen S. Structure 8:373-383(2000) [PubMed: 10801485] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND ASN-199, STRUCTURE OF CARBOHYDRATE.
[4]	"A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase." Moelgaard A., Larsen S. Acta Crystallogr. D 58:111-119(2002) [PubMed: 11752785] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND ASN-199, STRUCTURE OF CARBOHYDRATE.
[5]	"Short strong hydrogen bonds in proteins: a case study of rhamnogalacturonan acetylesterase." Langkilde A., Kristensen S.M., Lo Leggio L., Molgaard A., Jensen J.H., Houk A.R., Navarro Poulsen J.C., Kauppinen S., Larsen S. Acta Crystallogr. D 64:851-863(2008) [PubMed: 18645234] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 18-250, DISULFIDE BONDS, GLYCOSYLATION AT ASN-121 AND ASN-199.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X89714 Genomic DNA. Translation: CAA61858.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DEO	X-ray	1.55	A	18-250	[»]
1DEX	X-ray	1.90	A	18-250	[»]
1K7C	X-ray	1.12	A	18-250	[»]
1PP4	X-ray	2.50	A/B	18-250	[»]
3C1U	X-ray	1.33	A	18-250	[»]

ProteinModelPortal

Q00017.

SMR

Q00017. Positions 18-250.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16189.

Family and domain databases

InterPro

IPR013830. Esterase_SGNH_hydro-type.
IPR013831. Esterase_SGNH_hydro-type_subgr.
IPR001087. Lipase_GDSL.
[Graphical view]

Gene3D

G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.

Pfam

PF00657. Lipase_GDSL. 1 hit.
[Graphical view]

SUPFAM

SSF52266. Esterase_SGNH_hydro-type. 1 hit.

PROSITE

PS01098. LIPASE_GDSL_SER. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RHA1_ASPAC

Accession

Primary (citable) accession number: Q00017

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program