ID   RGLC_ASPOR              Reviewed;         695 AA.
AC   Q2U5P7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable rhamnogalacturonate lyase C;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglC; ORFNames=AO090113000057;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007166; BAE63118.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U5P7; -.
DR   SMR; Q2U5P7; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   EnsemblFungi; BAE63118; BAE63118; AO090113000057.
DR   VEuPathDB; FungiDB:AO090113000057; -.
DR   HOGENOM; CLU_016624_0_0_1; -.
DR   OMA; FITQTRA; -.
DR   Proteomes; UP000006564; Chromosome 5.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..695
FT                   /note="Probable rhamnogalacturonate lyase C"
FT                   /id="PRO_0000394380"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
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        638
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   695 AA;  77249 MW;  E6032805EBE4EE1A CRC64;
     MFLPSRKALA FLACLASHSV ALLTTSENST HFNLANDRFS IALAKSNGHI VDVQLDGQDL
     LGPVDGNAGK GPYLDCSCIP SGFWTPGSGA HLELINGTDS TGTAYGGLYM SATYAGTNQT
     LSQWFFLRGE ETGLHAFSRV TYFNETTPSL RSLGELRTLF RPSTDLWTHF STSDGNYGPK
     PLGSNSGLVV QDATTYIGNV TDDPYVSQYS DYFTKYTLAE SWRNHDVHGL FSDGSSSSDG
     STFGAWLVHN TVETYYGGPL HSDLVVDGIV YNYLVSGHHG APTPNLTHGF DRTWGPQFYY
     FNRGDSETTL ADLRADAAKY ADPEWNAEFY DSIADHIPNF TPSTGRTTFK GKVSLPKGAK
     RPIIVLSEDG QDFQLNVFNT ESLQYWAEID KSGSFSIPRV VEGTYRITIY ADEIFGWFIQ
     DHVKVLKSQS KDYSFTWKEE SAGKEIWRIG IPDKSSGEYL HGYAPDTSKP LQPEQHRIYW
     GKYDYPADFP EGINFHVGKS DPSQDLNYIH WAFFPSQGNH LRTEPYYDNV NNWTVTFDLT
     ADQLHNTNTA TFTVQIAGAK TANGNAKWTP VEGKYSNLPW TVNVNGRYES TWVIPYWRSG
     SCGVRSAVSC QNIEQKFAFP SKNLQEGKNE FVLSLPFNAS STETALLPDA LYVQARVMGS
     RLDPARPAPN PLVNSNLGFG RDNPIMEFSN NRIIT