ID   RGLA_EMENI              Reviewed;         527 AA.
AC   Q5AX45; C8VD91; Q1HFS0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=Rhamnogalacturonate lyase A;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rglA; ORFNames=AN7135;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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. Active against linseed rhamnogalacturonan.
CC       {ECO:0000269|PubMed:16844780}.
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; DQ490504; ABF50880.1; -; mRNA.
DR   EMBL; AACD01000122; EAA61387.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79004.1; -; Genomic_DNA.
DR   RefSeq; XP_664739.1; XM_659647.1.
DR   AlphaFoldDB; Q5AX45; -.
DR   SMR; Q5AX45; -.
DR   STRING; 227321.Q5AX45; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   GlyCosmos; Q5AX45; 3 sites, No reported glycans.
DR   EnsemblFungi; CBF79004; CBF79004; ANIA_07135.
DR   GeneID; 2870208; -.
DR   KEGG; ani:ANIA_07135; -.
DR   VEuPathDB; FungiDB:AN7135; -.
DR   eggNOG; ENOG502QTKY; Eukaryota.
DR   HOGENOM; CLU_037882_1_1_1; -.
DR   InParanoid; Q5AX45; -.
DR   OMA; FKIGDWD; -.
DR   OrthoDB; 114708at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IDA:UniProtKB.
DR   GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR   CDD; cd10317; RGL4_C; 1.
DR   CDD; cd10316; RGL4_M; 1.
DR   CDD; cd10320; RGL4_N; 1.
DR   FunFam; 2.60.120.260:FF:000102; Rhamnogalacturonate lyase A; 1.
DR   FunFam; 2.60.40.1120:FF:000017; Rhamnogalacturonate lyase A; 1.
DR   FunFam; 2.70.98.10:FF:000020; Rhamnogalacturonate lyase A; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR   PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 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; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE   2: Evidence at transcript level;
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..527
FT                   /note="Rhamnogalacturonate lyase A"
FT                   /id="PRO_0000394371"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   527 AA;  56381 MW;  D07A2C92955DB47D CRC64;
     MLSKTFLLSS AVLWARVANA AFGITDNGSS YTIDANSPNP LKFTVNKSSC DITSIVYYGS
     EFQYSGKGSH IGSGLGSATV SATQSGDYIK VTCDTSSLTH YFVVHNGDPI IHMATYITAE
     PDIGELRFIA RLNSNLLPNE EPFGDVSTTS GGSAIEGSDV FLVNGETRSK FYSSERFIDD
     HRHCISGSAH RVCMILNQYE SSSGGPFFRD INSNNGGDYN ALYWYMNSGH VQTESFRTGL
     HGPYSMYFSR SGTPSTNIDT SFFASLGIKG YVAANGRGTV TGKASGADSS MDWVVHWYNN
     DAQYWTYTAS DGSFTSPAMK PGTYTMKYYQ GEFPVAETTV TVSAGSSTTK NISGSVKTGT
     TIFKIGEWDG QPTGFRNADK QLRMHPSDSR MDSWSSTYTV GSSSLSDFPM AVFKSVNNPV
     TIKFTATSAQ TGAATLRIGT TLSFAGGRPQ ATINSYTGPA PSAPTNLNSR GVTRGAYRGL
     GEVYDVSVPA GTIVTGENTI TISVISGSSG DAFLSPNVVF DCIELFQ
//