ID A0A2G9HG13_9LAMI Unreviewed; 635 AA.
AC A0A2G9HG13;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=CDL12_10909 {ECO:0000313|EMBL:PIN16455.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN16455.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN16455.1}.
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DR EMBL; NKXS01001862; PIN16455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HG13; -.
DR STRING; 429701.A0A2G9HG13; -.
DR OrthoDB; 1215403at2759; -.
DR Proteomes; UP000231279; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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:SF10; 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, ECO:0000313|EMBL:PIN16455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 355..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 635 AA; 72273 MW; B2983C8A88295D03 CRC64;
MAIATTKLQD LVVIDNGVIQ LTLTNPGGLI RGIRYNGIDN LLELHNEDLN GGFWDLNWSE
AGSAKTRGKF DTIEGTSLRV IVENEEQIEL SFTRTWDPSV QGEQAPLRID RRFVMLRGCP
GFYSYAIFEH LEDFPGFNLN TTRIAFMLNK DKFHYMAVAD NRQRYMPLPD DRLPPRGQQL
AYPEAVLLVD PVEPEFKGEV DDKYQYSCEN KDNRVHGWIC FDPPVGFWQI TPSNEFRNGG
PFKQDLTSHV NPTTLAIFVT SHYAGEDLLL KFQPGEIWKK VFGPVFIYLN SVSDRDDALS
LWDDAKERMK IEVESWPYSF AASDDFPKSN QRGAIRGKLL VHDRYITEDA IPAEAAYVGL
ARPGDSGSWQ RESKGYQFWT TVDKNGYFAI NNIRTGNYNL YAWVPGFIGD YKFEAALTIN
PGCDIDVGEL TYKPPRNGPT LWEIGTPTRS ASEFYVPDPN PLYINKLYVN HPDRFRQYGL
WERYTDLYPE KDLVYTVGVS DYRKDWFYAQ VTRRIGNNAY KSTTWQIKFN IDNVVSGGTY
TLRLALASAH NSKLEVRVND ADANPPLFST GVIGGDNAIA RHGIHGLYWL FNVDIAAAQL
MQGENTIYLT QARSSSPFQG IMYDYIRLEC PSTNS
//
