ID   RGLB_ASPFC              Reviewed;         658 AA.
AC   B0XPA2;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Probable rhamnogalacturonate lyase B;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglB; ORFNames=AFUB_016620;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP56940.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XPA2; -.
DR   SMR; B0XPA2; -.
DR   EnsemblFungi; EDP56940; EDP56940; AFUB_016620.
DR   VEuPathDB; FungiDB:AFUB_016620; -.
DR   HOGENOM; CLU_016624_0_0_1; -.
DR   PhylomeDB; B0XPA2; -.
DR   Proteomes; UP000001699; 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; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..658
FT                   /note="Probable rhamnogalacturonate lyase B"
FT                   /id="PRO_0000394373"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   658 AA;  73532 MW;  EF11F6814D05C489 CRC64;
     MRFAIPLGAA CAWAGVALAA LQIAEDFSSI TLNNDRFKAV WSKSKGSVVD MFLDGQDLLG
     PQSGSTGIGP YLDCYCVPSG FYTAGATNPR MQYVEGTDST GTKYAGVILN DTYTPTGQQF
     QQYWFLRDGE TGLHMFSRLA YYNETTPFLR NLQEFRTLFR PNTQLWTHLT SSELQTAPLP
     SKNAVSKQVV VQDATWRFNN TPDDAYYTQF SEYFTKYTFS NQWRDNDVHG LYGDGTNSNG
     STYGAWLVMN TKGPLHSDLT VDGIVYNYIV SNHHGEGTPN ITNGFDRTFG PQFYLFNGGK
     GSTSSLQDLR SEAAKLADPS WNAEFYDSIA KHVVGYVPSS KRGSVDGRIK LPKGASNPIA
     ILTVDGQYFQ DNSVVPSSYQ YWTDIDTSGR FRIDRVVEGK YRLTVYADGI FGDFVRDGVT
     VRAGKTTTVK EKWDAESAGK EIWRLGTPDK SSGEFRHGVA RDPTHPLHPP EYLIYWGAYD
     WQSDFPKGID YTIGSSDPAT DFNTVHWSVF GPTPDNPNVE YNTTHDWKIN FSLTKKQLRN
     SKKATLTIQL AGAKTASGNT DEYKASEPYI NLIHESYIND QKEPLSFVIG FNQSSSCIVR
     SAVSCYQVRS RMEFPADWLK VGENTLTLHL PYNATDTETA ILPATVYVQY DALRLELD