ID A0A319C0L5_9EURO Unreviewed; 527 AA.
AC A0A319C0L5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Rhamnogalacturonate lyase {ECO:0000256|PIRNR:PIRNR011794};
DE EC=4.2.2.23 {ECO:0000256|PIRNR:PIRNR011794};
GN ORFNames=BO82DRAFT_393787 {ECO:0000313|EMBL:PYH79546.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH79546.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH79546.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH79546.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ821718; PYH79546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319C0L5; -.
DR STRING; 1448315.A0A319C0L5; -.
DR VEuPathDB; FungiDB:BO82DRAFT_393787; -.
DR OrthoDB; 66666at2759; -.
DR Proteomes; UP000248340; 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 Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR011794};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR011794}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT CHAIN 20..527
FT /note="Rhamnogalacturonate lyase"
FT /evidence="ECO:0000256|PIRNR:PIRNR011794"
FT /id="PRO_5016196707"
FT DOMAIN 21..269
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 275..348
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 360..525
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
FT DISULFID 49..92
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
FT DISULFID 183..192
FT /evidence="ECO:0000256|PIRSR:PIRSR011794-1"
SQ SEQUENCE 527 AA; 56158 MW; E35311F5DDD7C3F0 CRC64;
MLKASLLSFV AFTAQVANAA FGITTSSSAY VIDTNASTQL KFTVSRSSCD ITSIIHYGTE
LQYSSQGSHI GSGLGSATVT AVQSGDYIKV TCVTDTLTQY MVVHNGDPII HMATYITAEP
SIGELRFIAR LNSDVLPNEE PFGDVSTTAD GTAIEGSDVF LVGSETRSKF YSSERFIDDQ
RHCIAGDAHR VCMILNQYES SSGGPFHRDI NSNNGGSYNA LYWYMNSGHV QTESYRMGLH
GPYSMYFSRS GTPSTSIDTS FFADLDIQGY VAASGRGKVT 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
//
