Reviewed, UniProtKB/Swiss-Prot Q00001 (RHGA_ASPAC)

Names and origin

Protein names

Recommended name:
    Rhamnogalacturonase A
      Short name=RGase A
      Short name=RHG A
    EC=3.2.1.-

Gene names

Name:

rhgA

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	440 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	Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins.
Subcellular location	Secreted.
Post-translational modification	The N-terminus is blocked. N-glycosylated and may also be O-glycosylated.
Sequence similarities	Belongs to the glycosyl hydrolase 28 family.
biophysicochemical properties	pH dependence: Optimum pH is 3.5. Unstable above pH 6.0. Temperature dependence: Optimum temperature is 30-50 degrees Celsius.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	polygalacturonase activity 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 – 18

18

Chain

19 – 440

422

Rhamnogalacturonase A

PRO_0000024825

Sites

Active site

215

1

Proton donor By similarity

Active site

290

1

By similarity

Amino acid modifications

Glycosylation

50

1

N-linked (GlcNAc...)

Glycosylation

317

1

N-linked (GlcNAc...)

Glycosylation

385

1

O-linked (Man)

Glycosylation

386

1

O-linked (Man)

Glycosylation

388

1

O-linked (Man)

Glycosylation

389

1

O-linked (Man)

Glycosylation

390

1

O-linked (Man)

Glycosylation

391

1

O-linked (Man)

Glycosylation

392

1

O-linked (Man)

Glycosylation

394

1

O-linked (Man)

Glycosylation

398

1

O-linked (Man)

Glycosylation

401

1

O-linked (Man)

Glycosylation

403

1

O-linked (Man)

Glycosylation

404

1

O-linked (Man)

Glycosylation

416

1

O-linked (Man)

Glycosylation

418

1

O-linked (Man)

Glycosylation

423

1

O-linked (Man)

Glycosylation

426

1

O-linked (Man)

Glycosylation

427

1

O-linked (Man)

Glycosylation

436

1

O-linked (Man)

Disulfide bond

39 ↔ 65

Disulfide bond

217 ↔ 234

Disulfide bond

340 ↔ 346

Disulfide bond

368 ↔ 377

Experimental info

Sequence conflict

3

1

A → G in AAA64367. Ref.2

Sequence conflict

11

1

S → A in AAA64367. Ref.2

Sequence conflict

161

1

V → I in AAA64367. Ref.2

Secondary structure

1

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440

Helix Strand Turn

Details...

Helix

30 – 36

7

Beta strand

38 – 40

3

Helix

41 – 44

4

Beta strand

49 – 53

5

Helix

55 – 65

11

Beta strand

70 – 73

4

Beta strand

75 – 80

6

Beta strand

84 – 88

5

Beta strand

90 – 96

7

Beta strand

98 – 102

5

Beta strand

107 – 122

16

Beta strand

124 – 126

3

Beta strand

129 – 131

3

Helix

135 – 138

4

Turn

139 – 141

3

Beta strand

146 – 164

19

Beta strand

170 – 187

18

Beta strand

196 – 245

50

Beta strand

249 – 265

17

Beta strand

267 – 274

8

Beta strand

277 – 293

17

Beta strand

295 – 299

5

Beta strand

308 – 311

4

Beta strand

314 – 328

15

Turn

330 – 332

3

Beta strand

335 – 339

5

Beta strand

346 – 362

17

Beta strand

364 – 375

12

Beta strand

388 – 393

6

Beta strand

415 – 417

3

Sequences

	Sequence		Length	Mass (Da)
	Q00001-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3596371179A4F88F	FASTA	440	45,962
	10 20 30 40 50 60 MRALFLLALG SIPALVSGQL SGSVGPLTSA STKGATKTCN ILSYGAVADN STDVGPAITS 70 80 90 100 110 120 AWAACKSGGL VYIPSGNYAL NTWVTLTGGS ATAIQLDGII YRTGTASGNM IAVTDTTDFE 130 140 150 160 170 180 LFSSTSKGAV QGFGYVYHAE GTYGARILRL TDVTHFSVHD VILVDAPAFH FTMDTCSDGE 190 200 210 220 230 240 VYNMAIRGGN EGGLDGIDVW GSNIWVHDVE VTNKDECVTV KSPANNILVE SIYCNWSGGC 250 260 270 280 290 300 AMGSLGADTD VTDIVYRNVY TWSSNQMYMI KSNGGSGTVS NVLLENFIGH GNAYSLDIDG 310 320 330 340 350 360 YWSSMTAVAG DGVQLNNITV KNWKGTEANG ATRPPIRVVC SDTAPCTDLT LEDIAIWTES 370 380 390 400 410 420 GSSELYLCRS AYGSGYCLKD SSSHTSYTTT STVTAAPSGY SATTMAADLA TAFGLTASIP 430 440 IPTIPTSFYP GLTPYSALAG

References

[1]	"Cloning, sequence and expression of the gene coding for rhamnogalacturonase of Aspergillus aculeatus; a novel pectinolytic enzyme." Suykerbuyk M.E.G., Schaap P.J., Stam H., Musters W., Visser J. Appl. Microbiol. Biotechnol. 43:861-870(1995) [PubMed: 7576553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: CBS 115.80.
[2]	"Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus." Kofod L.V., Kauppinen S., Christgau S., Andersen L.N., Heldt-Hansen H.P., Doerreich K., Dalboege H. J. Biol. Chem. 269:29182-29189(1994) [PubMed: 7961884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: KSM 510.
[3]	"The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase." Azadi P., O'Neill M.A., Bergmann C., Darvill A.G., Albersheim P. Glycobiology 5:783-789(1995) [PubMed: 8720076] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix." Petersen T.N., Kauppinen S., Larsen S. Structure 5:533-544(1997) [PubMed: 9115442] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

S80208 Genomic DNA. Translation: AAB35485.1.
X83525 Genomic DNA. Translation: CAA58507.2.
L35499 mRNA. Translation: AAA64367.1.

PIR

A55415.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RMG	X-ray	2.00	A	19-440	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH28. Glycoside Hydrolase Family 28.

Family and domain databases

InterPro

IPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.

Pfam

PF00295. Glyco_hydro_28. 1 hit.
[Graphical view]

SMART

SM00710. PbH1. 3 hits.
[Graphical view]

PROSITE

PS00502. POLYGALACTURONASE. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RHGA_ASPAC

Accession

Primary (citable) accession number: Q00001
Secondary accession number(s): Q00018

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)