RHGA_ASPAC
ID RHGA_ASPAC Reviewed; 440 AA.
AC Q00001; Q00018;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Rhamnogalacturonase A;
DE Short=RGase A;
DE Short=RHG A;
DE EC=3.2.1.171;
DE AltName: Full=Rhamnogalacturonan hydrolase A;
DE Flags: Precursor;
GN Name=rhgA;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=CBS 115.80;
RX PubMed=7576553; DOI=10.1007/bf02431920;
RA Suykerbuyk M.E.G., Schaap P.J., Stam H., Musters W., Visser J.;
RT "Cloning, sequence and expression of the gene coding for
RT rhamnogalacturonase of Aspergillus aculeatus; a novel pectinolytic
RT enzyme.";
RL Appl. Microbiol. Biotechnol. 43:861-870(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=KSM 510;
RX PubMed=7961884; DOI=10.1016/s0021-9258(19)62028-4;
RA Kofod L.V., Kauppinen S., Christgau S., Andersen L.N., Heldt-Hansen H.P.,
RA Doerreich K., Dalboege H.;
RT "Cloning and characterization of two structurally and functionally
RT divergent rhamnogalacturonases from Aspergillus aculeatus.";
RL J. Biol. Chem. 269:29182-29189(1994).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8720076; DOI=10.1093/glycob/5.8.783;
RA Azadi P., O'Neill M.A., Bergmann C., Darvill A.G., Albersheim P.;
RT "The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved
RT by an endohydrolase and an endolyase.";
RL Glycobiology 5:783-789(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9115442; DOI=10.1016/s0969-2126(97)00209-8;
RA Petersen T.N., Kauppinen S., Larsen S.;
RT "The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus:
RT a right-handed parallel beta helix.";
RL Structure 5:533-544(1997).
RN [5]
RP FUNCTION.
RX PubMed=9464254; DOI=10.1006/bbrc.1997.8009;
RA Pitson S.M., Mutter M., van den Broek L.A., Voragen A.G., Beldman G.;
RT "Stereochemical course of hydrolysis catalysed by alpha-L-rhamnosyl and
RT alpha-D-galacturonosyl hydrolases from Aspergillus aculeatus.";
RL Biochem. Biophys. Res. Commun. 242:552-559(1998).
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectine lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Has a positive effect in the apple hot-mash
CC liquefaction process. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-
CC alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions
CC of pectins. {ECO:0000269|PubMed:9464254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic
CC bond in the rhamnogalacturonan I backbone with initial inversion of
CC anomeric configuration releasing oligosaccharides with beta-D-GalA at
CC the reducing end.; EC=3.2.1.171;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5. Unstable above pH 6.0.;
CC Temperature dependence:
CC Optimum temperature is 30-50 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: N-glycosylated and may also be O-glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; S80208; AAB35485.1; -; Genomic_DNA.
DR EMBL; X83525; CAA58507.2; -; Genomic_DNA.
DR EMBL; L35499; AAA64367.1; -; mRNA.
DR PIR; A55415; A55415.
DR PDB; 1RMG; X-ray; 2.00 A; A=19-440.
DR PDBsum; 1RMG; -.
DR AlphaFoldDB; Q00001; -.
DR SMR; Q00001; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; RHG28B_ASPAC; -.
DR KEGG; ag:AAA64367; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_34742; -.
DR BioCyc; MetaCyc:MON-16264; -.
DR BRENDA; 3.2.1.171; 488.
DR EvolutionaryTrace; Q00001; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..440
FT /note="Rhamnogalacturonase A"
FT /id="PRO_0000024825"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 385
FT /note="O-linked (Man) threonine"
FT CARBOHYD 386
FT /note="O-linked (Man) serine"
FT CARBOHYD 388
FT /note="O-linked (Man) threonine"
FT CARBOHYD 389
FT /note="O-linked (Man) threonine"
FT CARBOHYD 390
FT /note="O-linked (Man) threonine"
FT CARBOHYD 391
FT /note="O-linked (Man) serine"
FT CARBOHYD 392
FT /note="O-linked (Man) threonine"
FT CARBOHYD 394
FT /note="O-linked (Man) threonine"
FT CARBOHYD 398
FT /note="O-linked (Man) serine"
FT CARBOHYD 401
FT /note="O-linked (Man) serine"
FT CARBOHYD 403
FT /note="O-linked (Man) threonine"
FT CARBOHYD 404
FT /note="O-linked (Man) threonine"
FT CARBOHYD 416
FT /note="O-linked (Man) threonine"
FT CARBOHYD 418
FT /note="O-linked (Man) serine"
FT CARBOHYD 423
FT /note="O-linked (Man) threonine"
FT CARBOHYD 426
FT /note="O-linked (Man) threonine"
FT CARBOHYD 427
FT /note="O-linked (Man) serine"
FT CARBOHYD 436
FT /note="O-linked (Man) serine"
FT DISULFID 39..65
FT DISULFID 217..234
FT DISULFID 340..346
FT DISULFID 368..377
FT CONFLICT 3
FT /note="A -> G (in Ref. 2; AAA64367)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="S -> A (in Ref. 2; AAA64367)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="V -> I (in Ref. 2; AAA64367)"
FT /evidence="ECO:0000305"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1RMG"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1RMG"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 107..122
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1RMG"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1RMG"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 146..164
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 170..187
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 196..245
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 249..265
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 277..293
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 314..328
FT /evidence="ECO:0007829|PDB:1RMG"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 346..362
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1RMG"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1RMG"
SQ SEQUENCE 440 AA; 45962 MW; 3596371179A4F88F CRC64;
MRALFLLALG SIPALVSGQL SGSVGPLTSA STKGATKTCN ILSYGAVADN STDVGPAITS
AWAACKSGGL VYIPSGNYAL NTWVTLTGGS ATAIQLDGII YRTGTASGNM IAVTDTTDFE
LFSSTSKGAV QGFGYVYHAE GTYGARILRL TDVTHFSVHD VILVDAPAFH FTMDTCSDGE
VYNMAIRGGN EGGLDGIDVW GSNIWVHDVE VTNKDECVTV KSPANNILVE SIYCNWSGGC
AMGSLGADTD VTDIVYRNVY TWSSNQMYMI KSNGGSGTVS NVLLENFIGH GNAYSLDIDG
YWSSMTAVAG DGVQLNNITV KNWKGTEANG ATRPPIRVVC SDTAPCTDLT LEDIAIWTES
GSSELYLCRS AYGSGYCLKD SSSHTSYTTT STVTAAPSGY SATTMAADLA TAFGLTASIP
IPTIPTSFYP GLTPYSALAG
