ID   RGLA_NEOFI              Reviewed;         528 AA.
AC   A1D9P9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Probable rhamnogalacturonate lyase A;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglA; ORFNames=NFIA_029620;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027693; EAW20530.1; -; Genomic_DNA.
DR   RefSeq; XP_001262427.1; XM_001262426.1.
DR   AlphaFoldDB; A1D9P9; -.
DR   SMR; A1D9P9; -.
DR   STRING; 36630.CADNFIAP00002711; -.
DR   EnsemblFungi; EAW20530; EAW20530; NFIA_029620.
DR   GeneID; 4589193; -.
DR   KEGG; nfi:NFIA_029620; -.
DR   VEuPathDB; FungiDB:NFIA_029620; -.
DR   eggNOG; ENOG502QTKY; Eukaryota.
DR   HOGENOM; CLU_037882_1_1_1; -.
DR   OMA; DYIKVTC; -.
DR   OrthoDB; 195455at2759; -.
DR   Proteomes; UP000006702; 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   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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..528
FT                   /note="Probable rhamnogalacturonate lyase A"
FT                   /id="PRO_0000394372"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..193
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   528 AA;  56528 MW;  E1116A7263F4C3AA CRC64;
     MLSKATLLLS LPFWARVANA AFGITTTSSS YVIDANSASP LKFTVNRSNC DITSINFYGA
     ELQYQGTGSH IGSGLGSASV SATQSGDYIK VTCSTSTLTH YFVVHNGDPI IHMATHITAE
     PSIGELRFIA RLNNELLPNE EPFGQVSNTA GGTAIEGSDV YLVNGQTRSK FYSSERFIDD
     HRHCVSGSAH RVCMILNQYE SSSGGPFHRD INTNNGGQYN ALYWYMNSGH AQTEANRMGL
     HGPYSMYFSR SGTPGTNIDT SFFANLDIKG YVPANARGKV SGKASGADST FKWVVHWYND
     EAQYWTYTAS DGSFTSPAMK PGTYTMVYYQ GEYKVASTSV SVSAGSTTTK NISGSVTTGK
     TIFKIGEWDG QPTGFRNAAN QLRMHPSDSR MASWGPLTYT VGSSSLSDFP MAIFKSTNSP
     VTIKFTASSS QTGAATLRIG TTLSFAGGRP QAKVNSFTGP VPSAPKDLNS RGVTRGAYRG
     FGEVYDVAIP AGTIVAGTNT ITISVVSGSS GDTFLSPNFI FDCVELFQ