ID Q5KEU1_CRYNJ Unreviewed; 678 AA.
AC Q5KEU1;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN OrderedLocusNames=CNF04250 {ECO:0000313|EMBL:AAW44398.2};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW44398.2, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW44398.2, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; Evidence={ECO:0000256|ARBA:ARBA00001324};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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DR EMBL; AE017346; AAW44398.2; -; Genomic_DNA.
DR RefSeq; XP_571705.1; XM_571705.1.
DR AlphaFoldDB; Q5KEU1; -.
DR STRING; 214684.Q5KEU1; -.
DR CAZy; PL4; Polysaccharide Lyase Family 4.
DR PaxDb; 214684-Q5KEU1; -.
DR EnsemblFungi; AAW44398; AAW44398; CNF04250.
DR VEuPathDB; FungiDB:CNF04250; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_016624_1_0_1; -.
DR InParanoid; Q5KEU1; -.
DR OrthoDB; 1055596at2759; -.
DR Proteomes; UP000002149; Chromosome 6.
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 CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR PANTHER; PTHR32018:SF9; RHAMNOGALACTURONATE LYASE B; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..678
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006744931"
FT DOMAIN 371..443
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 461..674
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 678 AA; 75600 MW; 32C83A616ED1B4B7 CRC64;
MLKRLDLVTT ALLAVTGVAG KITYSETNDT ITLSSDRLTL GVNKTLGAMT GLEFDNVDVL
GPVSGRIGMG YFDCYCIPAV NTSVWTPDNP NPQSSRHYYV GQSQMASFEV HQGNDRNNNP
WIGLIMSETY EGTGQFFQQW WFLRDGEPGY HTFTRLQFDN GTEGIDLGNL QEFRQVISPN
SDIWTHLVTN DVQYGHLPSD EATGNQTTVQ DATWYYNITE GNPYRTESSD YFTKYEWADL
YGDHFAHGFY ADGTASNGST LGFWTVFNNL EGYTGGPLRS DLVVDTNIYN YYASNHRGAS
TMNITSGFDR IFGPTFIYLN KDGDLHNLYD DAKSYANTSF AADFYDDVAD LIPGYVNSSG
RGDFKAQISL PEGASNPKII LAQSGVDPQD NVDYTAKQYW TNVSSDGRVT IPRVQAGTYR
VTLYAEGIFG QFEQDEVVVS AGDGDGAEFR INWEAECHGI ELWRLGVPDK TAGEFLHGFA
KDPDHTLHQE EYREYWGAWD FPTDFPDGVN YTIGTSDPSK DWNYVHYSRY GGSFTRPEYV
LDNVNAWTVN WVPEGGLDVS GKTAALTVQL AGARTASGNL DLPEPTSNYS NVDYTVNVNG
NPLTWTILYN QSSSCSDRSG IACYNLRNVF TFPGEWLKND TNNVFEFALP YNASGGDVNF
RNYSISVLYD AIRLELSD
//
