ID   RGLA_ASPTN              Reviewed;         531 AA.
AC   Q0CVU1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable rhamnogalacturonate lyase A;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglA; ORFNames=ATEG_02193;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU37155.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476596; EAU37155.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001211371.1; XM_001211371.1.
DR   AlphaFoldDB; Q0CVU1; -.
DR   SMR; Q0CVU1; -.
DR   STRING; 341663.Q0CVU1; -.
DR   GeneID; 4316943; -.
DR   eggNOG; ENOG502QTKY; Eukaryota.
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   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..531
FT                   /note="Probable rhamnogalacturonate lyase A"
FT                   /id="PRO_0000394370"
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   531 AA;  56793 MW;  48128630F3AA9DC4 CRC64;
     MLSKALFFSS LPLWAKVASA AFGITTTDSS YTIDAGSPNP LKFTVSRSSC DITSINYYGS
     ELQYQSKGSH IGSGLGSASV SAVQNGDYIK VTCDTDTLTH YFVVHSGDPI IHMATYITAE
     PSIGELRFIA RLNSNLLPNE EPFGDVSTTA GGSAIEGSDV FLVNGQTRSK FYSSQRFIDD
     QRHCISGSAH RVCMILNQYE SSSGGPFHRD INSNNGGDYN SLYWYMNSGH VQTESYRMGL
     HGPYSMYFSR SGTPGTNIDT SFFANLDIKG YVPASGRGTV TGKASGADSN FKWVVHWYND
     AAQYWTYTAS DGSFTSPAMK PGTYTMAYYQ GEYRVAETSV TVSAGSSTTK NISGSVKTGT
     TIFKIGDWDG QPTGFLNADK QLRMHPSDSR MSSWGPVTYT VGSSSVGSFP MALFKSVNSP
     VTIKFTATSA QTGAATLRIG TTLSFAGGRP QATINSYTGP TPSAPTNLNS RGVTRGAYRG
     LGEVYDVSIP AGTIVAGTNT ITINVISGSS GDDFLSPNFV SAYPFLTLMR C