RHA1_ASPAC
ID RHA1_ASPAC Reviewed; 250 AA.
AC Q00017;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Rhamnogalacturonan acetylesterase;
DE Short=RGAE;
DE EC=3.1.1.86;
DE Flags: Precursor;
GN Name=rha1;
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], PROTEIN SEQUENCE OF 18-45, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=KSM 510;
RX PubMed=7592973; DOI=10.1074/jbc.270.45.27172;
RA Kauppinen S., Christgau S., Kofod L.V., Halkier T., Doerreich K.,
RA Dalboege H.;
RT "Molecular cloning and characterization of a rhamnogalacturonan
RT acetylesterase from Aspergillus aculeatus. Synergism between
RT rhamnogalacturonan degrading enzymes.";
RL J. Biol. Chem. 270:27172-27178(1995).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=9757128; DOI=10.1107/s0907444998004132;
RA Moelgaard A., Petersen J.F.W., Kauppinen S., Dalboege H., Johnsen A.H.,
RA Navarro Poulsen J.-C., Larsen S.;
RT "Crystallization and preliminary X-ray diffraction studies of the
RT heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from
RT Aspergillus aculeatus.";
RL Acta Crystallogr. D 54:1026-1029(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND
RP ASN-199, STRUCTURE OF CARBOHYDRATE, AND ACTIVE SITE.
RX PubMed=10801485; DOI=10.1016/s0969-2126(00)00118-0;
RA Moelgaard A., Kauppinen S., Larsen S.;
RT "Rhamnogalacturonan acetylesterase elucidates the structure and function of
RT a new family of hydrolases.";
RL Structure 8:373-383(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND
RP ASN-199, AND STRUCTURE OF CARBOHYDRATE.
RX PubMed=11752785; DOI=10.1107/s0907444901018479;
RA Moelgaard A., Larsen S.;
RT "A branched N-linked glycan at atomic resolution in the 1.12 A structure of
RT rhamnogalacturonan acetylesterase.";
RL Acta Crystallogr. D 58:111-119(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 18-250, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-121 AND ASN-199.
RX PubMed=18645234; DOI=10.1107/s0907444908017083;
RA Langkilde A., Kristensen S.M., Lo Leggio L., Molgaard A., Jensen J.H.,
RA Houk A.R., Navarro Poulsen J.C., Kauppinen S., Larsen S.;
RT "Short strong hydrogen bonds in proteins: a case study of
RT rhamnogalacturonan acetylesterase.";
RL Acta Crystallogr. D 64:851-863(2008).
CC -!- FUNCTION: Plays a key role in the degradation of rhamnogalacturonan in
CC the cell wall. Acts in synergy together with rhamnogalacturonase A
CC (RGase A) and rhamnogalacturonase B (RGase B).
CC {ECO:0000269|PubMed:7592973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of
CC alpha-D-galacturonic acid in rhamnogalacturonan I.; EC=3.1.1.86;
CC Evidence={ECO:0000269|PubMed:7592973};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0.;
CC -!- PTM: Carbohydrate at Asn-199 is composed of GlcNAc and Man.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; X89714; CAA61858.1; -; Genomic_DNA.
DR PDB; 1DEO; X-ray; 1.55 A; A=18-250.
DR PDB; 1DEX; X-ray; 1.90 A; A=18-250.
DR PDB; 1K7C; X-ray; 1.12 A; A=18-250.
DR PDB; 1PP4; X-ray; 2.50 A; A/B=18-250.
DR PDB; 3C1U; X-ray; 1.33 A; A=18-250.
DR PDBsum; 1DEO; -.
DR PDBsum; 1DEX; -.
DR PDBsum; 1K7C; -.
DR PDBsum; 1PP4; -.
DR PDBsum; 3C1U; -.
DR AlphaFoldDB; Q00017; -.
DR SMR; Q00017; -.
DR iPTMnet; Q00017; -.
DR KEGG; ag:CAA61858; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_53138; -.
DR BioCyc; MetaCyc:MON-16189; -.
DR BRENDA; 3.1.1.86; 488.
DR EvolutionaryTrace; Q00017; -.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR037459; RhgT-like.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:7592973"
FT CHAIN 18..250
FT /note="Rhamnogalacturonan acetylesterase"
FT /id="PRO_0000017852"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10801485"
FT ACT_SITE 209
FT /evidence="ECO:0000269|PubMed:10801485"
FT ACT_SITE 212
FT /evidence="ECO:0000269|PubMed:10801485"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10801485,
FT ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:10801485,
FT ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234"
FT DISULFID 105..113
FT /evidence="ECO:0000269|PubMed:18645234"
FT DISULFID 231..249
FT /evidence="ECO:0000269|PubMed:18645234"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1K7C"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1K7C"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1K7C"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1K7C"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:1K7C"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:1K7C"
SQ SEQUENCE 250 AA; 26351 MW; C30676A3A876A38B CRC64;
MKTAALAPLF FLPSALATTV YLAGDSTMAK NGGGSGTNGW GEYLASYLSA TVVNDAVAGR
SARSYTREGR FENIADVVTA GDYVIVEFGH NDGGSLSTDN GRTDCSGTGA EVCYSVYDGV
NETILTFPAY LENAAKLFTA KGAKVILSSQ TPNNPWETGT FVNSPTRFVE YAELAAEVAG
VEYVDHWSYV DSIYETLGNA TVNSYFPIDH THTSPAGAEV VAEAFLKAVV CTGTSLKSVL
TTTSFEGTCL
