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Database: UniProt
Entry: V7AZL5_PHAVU
LinkDB: V7AZL5_PHAVU
Original site: V7AZL5_PHAVU 
ID   V7AZL5_PHAVU            Unreviewed;       636 AA.
AC   V7AZL5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=PHAVU_009G144900g {ECO:0000313|EMBL:ESW09651.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW09651.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|EMBL:ESW09651.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
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; CM002296; ESW09651.1; -; Genomic_DNA.
DR   EMBL; CM002296; ESW09652.1; -; Genomic_DNA.
DR   RefSeq; XP_007137657.1; XM_007137595.1.
DR   RefSeq; XP_007137658.1; XM_007137596.1.
DR   AlphaFoldDB; V7AZL5; -.
DR   STRING; 3885.V7AZL5; -.
DR   EnsemblPlants; ESW09651; ESW09651; PHAVU_009G144900g.
DR   EnsemblPlants; ESW09652; ESW09652; PHAVU_009G144900g.
DR   GeneID; 18620161; -.
DR   Gramene; ESW09651; ESW09651; PHAVU_009G144900g.
DR   Gramene; ESW09652; ESW09652; PHAVU_009G144900g.
DR   eggNOG; ENOG502QQM5; Eukaryota.
DR   OMA; WLYHVNI; -.
DR   OrthoDB; 1215403at2759; -.
DR   Proteomes; UP000000226; Chromosome 9.
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; IPR010325; Rhamnogal_lyase.
DR   PANTHER; PTHR32018:SF8; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR   PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR   Pfam; PF14683; CBM-like; 1.
DR   Pfam; PF14686; fn3_3; 1.
DR   Pfam; PF06045; Rhamnogal_lyase; 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   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          354..426
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          440..628
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   636 AA;  72479 MW;  11C99F609DA19BBC CRC64;
     MSGPGVRLHI QDHHVVMDNG IVQVTLSNPG GIVTGIRYNG VDNLLEVLNK ESNRGYWDLV
     WSAPGTKGIF DVIQGTCFKV IVQNEEQVEL SFTRMWDPSL EGKFVPLNID KRFIMLRGSS
     GFYSYGIYEH LNGWPDFDLS ETRITFKLRK DKFQYMAMAD NRRRILPYPE DRLPGRCQTL
     GYAEAVLLTN PKDPQLQGEV DDKYQYSCAN MDNRVHGWIS FNPPVGFWQI TPSDEFRSGG
     PLKQNLTSHV GPTTLAMFLS SHYAGQDLVP KIRGGESWKK VFGPVYIYLN SAAVSDDPLW
     LWEDAKIQMM NEVQSWPYYF PASEDFLKSD QRGNISGRLL VLDKYICTDL ISANGAYVGL
     APPGDAGSWQ RECKDYQFWT RADENGFFTI RNVRPGDYNL FAWVPGFVGD YKFVDFMKIT
     PGSYTELGEL VYEPPRDGPT LWEIGIPDRS AAEFYAPDPN PQYMNRLFIN HPDRFRQYGL
     WDRYTELYPA TDLVYTVGVN DYRKDWFYAQ APRKKEDNTL QGTTWQIKFE LSGVVRGSTY
     KLRVAIASAT LAELQVRVND PNAGRPLFTS GLIGRDNSIA RLGIHGIYWL YNVSIPGSLL
     IDGTNTIYFT QPRCTSPFQG IMYDYIRLEG PPCEGI
//
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