ID G7XJD9_ASPKW Unreviewed; 528 AA.
AC G7XJD9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Rhamnogalacturonate lyase {ECO:0000256|PIRNR:PIRNR011794};
DE EC=4.2.2.23 {ECO:0000256|PIRNR:PIRNR011794};
GN ORFNames=AKAW_05278 {ECO:0000313|EMBL:GAA87164.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA87164.1};
RN [1] {ECO:0000313|EMBL:GAA87164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA87164.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; Evidence={ECO:0000256|ARBA:ARBA00001324,
CC ECO:0000256|PIRNR:PIRNR011794};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR011794}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418, ECO:0000256|PIRNR:PIRNR011794}.
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DR EMBL; DF126458; GAA87164.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XJD9; -.
DR STRING; 1033177.G7XJD9; -.
DR VEuPathDB; FungiDB:AKAW_05278; -.
DR eggNOG; ENOG502QTKY; Eukaryota.
DR InParanoid; G7XJD9; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10317; RGL4_C; 1.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 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; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR011794-1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR011794};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR011794};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR011794};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR011794}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT CHAIN 21..528
FT /note="Rhamnogalacturonate lyase"
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT /id="PRO_5010009660"
FT DOMAIN 22..270
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 277..349
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 361..526
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
FT DISULFID 50..93
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
FT DISULFID 184..193
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
SQ SEQUENCE 528 AA; 57086 MW; 704D66B885A3F4AE CRC64;
MLFRTSLLSL LSLAAGVVNA DFGITTNDDS YVINANSPNS LVFTVDRGSC DITSIVHYGT
ELQYSGKGSH IGSGLGTATV SATKSGDYIK VTCETDTLTQ YMVVHDGDPI IHMATYITEE
PSIGELRFIA RLNPDELPNE EPFGDVSNTA GGEAIEGSDV FLVDGETRSK FYSSQRFIDD
QRHCIAGDEH RVCMILNQYE TSSGGPFHRD INSNNGGDYN SLYWYMNSGH VQTESYRMGL
HGPYSMYFSR SGTPSTDIDT SFFADLDIEG YVAEADRGTV SGTASGADSS FDWVVHWYND
DAQYWTYTSS SGSFTSPAMK PGTYTMVYYQ GEYVVATSEV TVSAGSSTTK NISGSVKTGT
TIFKIGDWDG QPTGFRNAEN QLRMHPSDSR MSDWGPLTYT VGSSSLTDFP MAVFKAVNDP
VTIKFTATSD QTGAATLRIG TTLSFAGGRP QATINDYEGS APSAPTNLNS RGVTRGAYRG
YGEVYDVSVP EGTIVEGENT ITISVISGSS GDEFLSPNFI FDCVELFQ
//
