RGLB_ASPTN
ID RGLB_ASPTN Reviewed; 660 AA.
AC Q0C7K7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Probable rhamnogalacturonate lyase B;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglB; ORFNames=ATEG_10327;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone
CC of pectin (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
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DR EMBL; CH476610; EAU29324.1; -; Genomic_DNA.
DR RefSeq; XP_001218675.1; XM_001218674.1.
DR AlphaFoldDB; Q0C7K7; -.
DR SMR; Q0C7K7; -.
DR EnsemblFungi; EAU29324; EAU29324; ATEG_10327.
DR GeneID; 4354631; -.
DR VEuPathDB; FungiDB:ATEG_10327; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_016624_0_0_1; -.
DR OMA; HGEGTPN; -.
DR OrthoDB; 195455at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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 Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Lyase; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..660
FT /note="Probable rhamnogalacturonate lyase B"
FT /id="PRO_0000394377"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 660 AA; 73513 MW; 36C109D402FD2506 CRC64;
MRLSVSLGLA SLWTAIGATA LNVSQTNSSI TLANDRLTAI FSNAGKVVDL YLDGQDLLGP
ASGSTGVGPY LDCYCTPKGF YTAGSTTPRM EVVQGTDATG TQYAGVILND TYTPTGQQFQ
QYWFLRDGET GLHMFSRLAY YNETTPFLRN LQEFRTLFRP NTDLWTHLTS SELQTAPLPS
DEAVGKQVVV QDATWRFNNT PNDAYYTQFS EYFTKYTFSN AWRDNNVHGL YADGSTSNGT
TFGAWLVMNT KDTYYGGPLH SDLTVDGIVY NYIVSNHHGE GTPNITNGFD RTFGPQFYLF
NGGGSSSLNE LRSEAESLAD PSWNVEFYDS IAKHVVGYVP SSKRGSVQGQ IKLPRGATRP
IAILTVDGQY FQDNSVDPRS YQYWVEMDAN GKFQLDHVVE GKYRLTVYAD GIFGDYVRDG
VQVRGRKTTR INDSWQPESA GVEVWRLGTP DKSSGEFLHG VARDPTHPLH PPEYLIYWGA
YDWQQDFPNG VNYTIGSSDP ATDFNTVHWS VFGPTPDNPD VEYDTTHDWA INFSLTKKQL
QKRKTATLTI QLAGAKTASG NTDVYKPDEP YTNLALESYI NQQEEPLTML IGFNQSSSCI
VRSAVSCYQV RSRMTFPADW LQVGSNTLTL HLPRNATDVE DAILPGTVYV QYDALRLELS
