RGLA_ASPAC
ID RGLA_ASPAC Reviewed; 527 AA.
AC Q00019;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Rhamnogalacturonate lyase A;
DE EC=4.2.2.23;
DE AltName: Full=Rhamnogalacturonan lyase;
DE Flags: Precursor;
GN Name=rglA; Synonyms=RGL4;
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 [MRNA].
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 [2]
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 [3]
RP FUNCTION.
RX PubMed=8587995; DOI=10.1104/pp.110.1.73;
RA Mutter M., Colquhoun I.J., Schols H.A., Beldman G., Voragen A.G.;
RT "Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan
RT alpha-L-rhamnopyranosyl-(1-->4)-alpha-D-galactopyranosyluronide lyase.";
RL Plant Physiol. 110:73-77(1996).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9576783; DOI=10.1104/pp.117.1.141;
RA Mutter M., Colquhoun I.J., Beldman G., Schols H.A., Bakx E.J.,
RA Voragen A.G.;
RT "Characterization of recombinant rhamnogalacturonan alpha-L-
RT rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from
RT Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I
RT regions of pectin.";
RL Plant Physiol. 117:141-152(1998).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=12136151; DOI=10.1107/s0907444902009137;
RA Kadirvelraj R., Harris P., Poulsen J.C., Kauppinen S., Larsen S.;
RT "A stepwise optimization of crystals of rhamnogalacturonan lyase from
RT Aspergillus aculeatus.";
RL Acta Crystallogr. D 58:1346-1349(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 20-527, AND DISULFIDE BOND.
RX PubMed=15135077; DOI=10.1016/j.febslet.2004.03.094;
RA McDonough M.A., Kadirvelraj R., Harris P., Poulsen J.C., Larsen S.;
RT "Rhamnogalacturonan lyase reveals a unique three-domain modular structure
RT for polysaccharide lyase family 4.";
RL FEBS Lett. 565:188-194(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 20-527 OF MUTANTS ALA-169 AND
RP ALA-229, DISULFIDE BOND, AND FUNCTION.
RX PubMed=20851126; DOI=10.1016/j.jmb.2010.09.013;
RA Jensen M.H., Otten H., Christensen U., Borchert T.V., Christensen L.L.,
RA Larsen S., Leggio L.L.;
RT "Structural and biochemical studies elucidate the mechanism of
RT rhamnogalacturonan lyase from Aspergillus aculeatus.";
RL J. Mol. Biol. 404:100-111(2010).
CC -!- FUNCTION: Pectinolytic enzyme that has a positive effect in the apple
CC hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-
CC rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage
CC by beta-elimination, thereby generating oligosaccharides terminating at
CC the non-reducing end with a hex-4-enopyranosyluronic acid residue.
CC {ECO:0000269|PubMed:20851126, ECO:0000269|PubMed:8587995,
CC ECO:0000269|PubMed:9576783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0, enzymatic activity becomes unstable below this
CC value. {ECO:0000269|PubMed:9576783};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:9576783};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
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DR EMBL; L35500; AAA64368.1; -; mRNA.
DR PIR; B55415; B55415.
DR PDB; 1NKG; X-ray; 1.50 A; A=20-527.
DR PDB; 2XHN; X-ray; 1.52 A; A/B=20-527.
DR PDB; 3NJV; X-ray; 2.40 A; A=20-527.
DR PDB; 3NJX; X-ray; 1.94 A; A=20-527.
DR PDBsum; 1NKG; -.
DR PDBsum; 2XHN; -.
DR PDBsum; 3NJV; -.
DR PDBsum; 3NJX; -.
DR AlphaFoldDB; Q00019; -.
DR SMR; Q00019; -.
DR CAZy; PL4; Polysaccharide Lyase Family 4.
DR KEGG; ag:AAA64368; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_35293; -.
DR BioCyc; MetaCyc:MON-16403; -.
DR BRENDA; 4.2.2.23; 488.
DR EvolutionaryTrace; Q00019; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10316; RGL4_M; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR InterPro; IPR016590; Rhamnogalacturonase_B.
DR InterPro; IPR015364; RhgB_N.
DR PANTHER; PTHR36574; PTHR36574; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 1.
DR PIRSF; PIRSF011794; Rhamnogalacturonase_B; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Lyase; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..19
FT CHAIN 20..527
FT /note="Rhamnogalacturonate lyase A"
FT /id="PRO_0000024912"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..92
FT DISULFID 183..192
FT MUTAGEN 169
FT /note="K->A: Impairs enzyme activity."
FT MUTAGEN 229
FT /note="H->A: Impairs enzyme activity."
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1NKG"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1NKG"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1NKG"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 238..250
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1NKG"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:1NKG"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 434..444
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 448..453
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 495..505
FT /evidence="ECO:0007829|PDB:1NKG"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1NKG"
FT STRAND 515..526
FT /evidence="ECO:0007829|PDB:1NKG"
SQ SEQUENCE 527 AA; 56190 MW; B0E14412E5CDC080 CRC64;
MLKASLLSFV AFTAQVAHAA FGITTSSSAY VIDTNAPNQL KFTVSRSSCD ITSIIHYGTE
LQYSSQGSHI GSGLGSATVT ATQSGDYIKV TCVTDTLTQY MVVHNGDPII HMATYITAEP
SIGELRFIAR LNSDLLPNEE PFGDVSTTAD GTAIEGSDVF LVGSETRSKF YSSERFIDDQ
RHCIAGDAHR VCMILNQYES SSGGPFHRDI NSNNGGSYNA LYWYMNSGHV QTESYRMGLH
GPYSMYFSRS GTPSTSIDTS FFADLDIKGY VAASGRGKVA GTASGADSSM DWVVHWYNDA
AQYWTYTSSS GSFTSPAMKP GTYTMVYYQG EYAVATSSVT VSAGSTTTKN ISGSVKTGTT
IFKIGEWDGQ PTGFRNAANQ LRMHPSDSRM SSWGPLTYTV GSSALTDFPM AVFKSVNNPV
TIKFTATSAQ TGAATLRIGT TLSFAGGRPQ ATINSYTGSA PAAPTNLDSR GVTRGAYRGL
GEVYDVSIPS GTIVAGTNTI TINVISGSSG DTYLSPNFIF DCVELFQ
