ID Q5H3Y9_XANOR Unreviewed; 567 AA.
AC Q5H3Y9;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN Name=rhgB {ECO:0000313|EMBL:AAW74332.1};
GN OrderedLocusNames=XOO1078 {ECO:0000313|EMBL:AAW74332.1};
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW74332.1, ECO:0000313|Proteomes:UP000006735};
RN [1] {ECO:0000313|EMBL:AAW74332.1, ECO:0000313|Proteomes:UP000006735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(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; AE013598; AAW74332.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5H3Y9; -.
DR STRING; 291331.XOO1078; -.
DR KEGG; xoo:XOO1078; -.
DR HOGENOM; CLU_037882_1_1_6; -.
DR Proteomes; UP000006735; 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 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000006735};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 61..302
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 320..386
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 401..564
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 60857 MW; EAF8B0D2C806FDC7 CRC64;
MLEVRTVRTF SVSDARLASR AGIATKSCFR TVTTMPRHRL HTFACALLLY AGVSAPALAE
FGCTRSGDRV IVDSGAELVF SVDTHDGDIV SMRYRDNELQ TTEPKGSQIA SGLGSASVDA
RIAGGTIIVS AKAGDLIQYY IVRKGRNAIY MATYAPTLPP VGELRFVARL NVSKLPDAQQ
EPDSNVGTAI EGNDVFLLPD GRTSSKFYSA RRMMDDQVHG VSGPGVAVFM LMGNREHSAG
GPFFKDIATQ KTRVTHELYN YMYSDHTQTE AFRGGLHGVY GLLFTDGSAP SDAQLNTDFV
DATLGLSDYL PASGRGAVGG QVSGVLPDQP AVIGLCNAQA QYWATADGSG EYQVTGVRPG
RYRMTLYQNE LEVAWRDIEV FANDTAHATL QAVALPGTLK WQIGIPDGTP AGFGYADLLP
HAHPSDARMR WSATTYTVGS SGQSSFPAVQ WRGINTPSRI DFTLAADEVR DYRLRIFVPL
AQGSARPQIS VNARWNGPMP DAPLQPKTRG ITRGTTRGNN ALYEMDIPAS ALQAGSNCIE
IGIASGSPDN GFLSPAIVFD SIQLVAL
//