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Database: UniProt
Entry: D2UCZ7_XANAP
LinkDB: D2UCZ7_XANAP
Original site: D2UCZ7_XANAP 
ID   D2UCZ7_XANAP            Unreviewed;       534 AA.
AC   D2UCZ7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   OrderedLocusNames=XALc_0866 {ECO:0000313|EMBL:CBA15384.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA15384.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA15384.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
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; FP565176; CBA15384.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2UCZ7; -.
DR   STRING; 380358.XALC_0866; -.
DR   KEGG; xal:XALC_0866; -.
DR   eggNOG; COG4625; Bacteria.
DR   Proteomes; UP000001890; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd10317; RGL4_C; 1.
DR   CDD; cd10316; RGL4_M; 1.
DR   CDD; cd10320; RGL4_N; 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   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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CBA15384.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..534
FT                   /note="rhamnogalacturonan endolyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003037543"
FT   DOMAIN          27..274
FT                   /note="Rhamnogalacturonase B N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09284"
FT   DOMAIN          280..353
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          367..531
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
FT   REGION          458..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  57029 MW;  2D7F3AD0A98A680E CRC64;
     MRTFFPLILC CIAVGGALPA AAQNGTFGLS HSGGRFVVDS GANLVFSVDD SNGDLVSMRY
     RGTELQSTEA KGSQIASGLG TATVAARTVG DTIVISAQAG DLIHYYMAHK GRNAIYMATY
     APTLLPIGEL RFVTRLNVNI LPNADHEPDS NVGTAIEAQD VFLLPDGRTS SKFYSARRAI
     EDSIHGVSGT NVAVRMWMGN REYSSGGPFF KDIATQKTVV THELYNYMFS NHTQTESYRG
     GLHGVYALLF TDGGAAPAAA TDLSFVDATL KLKGFLDSTG RGTVSGQASG VADGQPAVVG
     LSNDHAQYWA SADSTGQFKI AGVCPGHYRI TLYQNELEVA HDTLEVAAGS TAQATLQAVP
     LQGQVQWQIG LPDGTPGAFR NASLLPTMHP SDQRMASWGP LTYRVGTNAL EDFPAVQWHG
     VNAPTRIEFV LGADQVRDYR LRMFVPLTQA SARPQVSVND QWTGPMPPRP DQPNSRGITR
     GTYRGNNTVY LVDIPATALQ AGLNWVDIDV VSGSPDNGFL GPAVVFDSVQ LIVP
//
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