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Database: UniProt
Entry: A0A069DGP3_9BACL
LinkDB: A0A069DGP3_9BACL
Original site: A0A069DGP3_9BACL 
ID   A0A069DGP3_9BACL        Unreviewed;       543 AA.
AC   A0A069DGP3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=TCA2_4066 {ECO:0000313|EMBL:GAK41575.1};
OS   Paenibacillus sp. TCA20.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK41575.1, ECO:0000313|Proteomes:UP000028160};
RN   [1] {ECO:0000313|EMBL:GAK41575.1, ECO:0000313|Proteomes:UP000028160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCA20 {ECO:0000313|EMBL:GAK41575.1,
RC   ECO:0000313|Proteomes:UP000028160};
RA   Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA   Narumi I., Ito M.;
RT   "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT   Isolated from a Hot Spring Containing a High Concentration of Calcium
RT   Ions.";
RL   Genome Announc. 2:e00866-14(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAK41575.1}.
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DR   EMBL; BBIW01000008; GAK41575.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069DGP3; -.
DR   eggNOG; COG4625; Bacteria.
DR   Proteomes; UP000028160; Unassembled WGS sequence.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028160};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          37..282
FT                   /note="Rhamnogalacturonase B N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09284"
FT   DOMAIN          296..361
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          376..541
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   543 AA;  57545 MW;  EF2E94AFBAAC54A0 CRC64;
     MDNRFVKRMV SFFLILVMVG AAVLYPADKG YAATVYVTDN GTSIVVNTGS GLEYTVNKDN
     GDITSAKMNG TELSSSGGKG SHIASGLGSA ANVTWSKSPS GSTVLITVAT DTLTHYYSSR
     GGENTIYMAT YVTAQPSVGE LRYIFRGNGN VLTGVPANSN NRGTTGAIES QDVFGHSNGQ
     TTSKYYGNDQ AKDLTIRGAT GNGVGVFMAY GNREKSSGGP FFRDIQFQSG GDTEIYNYMN
     SGHAQTENWR MGLHGPYALV FTTGSTPAVP DFSWMSGLNL QGWVSSRGNV VLNGLSGMDS
     AYTYTIGFAN SNAQYWATAS SSGSASKYGM IPGTYTMTVY KGELAVYTEN VTVNANATTT
     VNTRTINNDP SAASAIWRIG NWDGTPRELL NGQTIPVRHP SDSRNPSWGP VTYAVGGATN
     KFPAIQFRGE NSPTTVTFNL NSSQAASAHV LKIGITAAYN NGRPSVTING NTLSNPAASS
     QPNSRSFTIG TYRGNNATFT WNIPASYFNN GANTLTITPI SGSSDLGNWL SAGWVYDAVE
     LLN
//
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