RGLA_ASPFU
ID RGLA_ASPFU Reviewed; 528 AA.
AC Q4W9T6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Probable rhamnogalacturonate lyase A;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglA; ORFNames=AFUA_4G03780;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000016; EAL84527.1; -; Genomic_DNA.
DR RefSeq; XP_746565.1; XM_741472.1.
DR AlphaFoldDB; Q4W9T6; -.
DR SMR; Q4W9T6; -.
DR STRING; 746128.CADAFUBP00009644; -.
DR EnsemblFungi; EAL84527; EAL84527; AFUA_4G03780.
DR GeneID; 3503929; -.
DR KEGG; afm:AFUA_4G03780; -.
DR VEuPathDB; FungiDB:Afu4g03780; -.
DR eggNOG; ENOG502QTKY; Eukaryota.
DR HOGENOM; CLU_037882_1_1_1; -.
DR InParanoid; Q4W9T6; -.
DR OMA; DYIKVTC; -.
DR OrthoDB; 195455at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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; IBA:GO_Central.
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:0045490; P:pectin catabolic process; IBA:GO_Central.
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_0000394367"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
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; 56736 MW; E0B22BB3995084E4 CRC64;
MLSKATLLLF LPSWARVTYA AFGITTTSSS YVIDANSPNP LKFTVNRSNC DITSINFYGA
ELQYQGTGSH IGSGLGSASV SATQSGDYIK VTCSTSTLTH YFVVHNGDPI IHMATYITAE
PSIGELRFIA RLNNELLPNE EPFGEVSNTS GGTAIEGSDV FLVNGQTRSK FYSSERFIDD
HRHCVSGSAH RVCMILNQYE SSSGGPFHRD INTNNGGQYN ALYWYMNSGH VQTEANRMGL
HGPYSMYFSR SGTPGTNIDT SFFANLDIQG YVPDSARGKV SGKASGADST FKWVVHWYND
EAQYWTYTAS DGSFTSPAMK PGTYTMVYYQ GEYKVASTSV SVSAGSTTTK NISGSVTTGK
TIFKIGEWDG QPTGFRNAAN QLRMHPSDSR MSSWGPLTYT VGSSSLSDFP MAIFKSVNSP
VTIKFTASSS QTGAATLRIG TTLSFAGGRP QVTVNSWTGP IPSAPKDLNS RGVTRGAYRG
LGEVYDVAIP AGTIVAGTNT ITISVVSGSS GDAFLSPNFI FDCVELFQ
