ID A0A1S3ZTM1_TOBAC Unreviewed; 639 AA.
AC A0A1S3ZTM1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN Name=LOC107790313 {ECO:0000313|RefSeq:XP_016467717.1,
GN ECO:0000313|RefSeq:XP_016467718.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016467717.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016467717.1, ECO:0000313|RefSeq:XP_016467718.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_016467717.1; XM_016612231.1.
DR RefSeq; XP_016467718.1; XM_016612232.1.
DR STRING; 4097.A0A1S3ZTM1; -.
DR PaxDb; 4097-A0A1S3ZTM1; -.
DR GeneID; 107790313; -.
DR KEGG; nta:107790313; -.
DR OMA; METHIGQ; -.
DR OrthoDB; 1215403at2759; -.
DR Proteomes; UP000084051; Unplaced.
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:SF39; OS11G0134100 PROTEIN; 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|RefSeq:XP_016467717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 358..430
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 444..632
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 639 AA; 72851 MW; 13608529694A614C CRC64;
MTAPGVQLHL PDDHHVVMDN GILQVTLSVP AGIVTRIKYN GVDNLLEILN DETNRGYWDV
VWSPAGTTGT TGTFERLICT TYKVILETDD QIELSFSREW DVSLQDKLIP LNIDKRFIML
KGSSGFYSYA IYEHLEGWPG FNLDETRIAF KLRKDKFHYM AMADNRQRYM PLPDDRLPDR
GQPLAYPEAV LLVNPVEPEF KGEVDDKYQY SCEDKDLKVH GWICMDPPLG FWIIIPSDEF
RSGGPLKQNL TSHVGPTALS MFLSAHYAGE DLVAKFGEGE PWKKVFGPVF IYLNYVNEGE
DPLILWEDAK EQMLVEVQSW PYSFPASEDF PSSSQRGNIS GRLLVQDRYF KDDKISASGA
YVGLAPPGEV GSWQRECKDY QFWIKADEEG YYIISDIRAG NYNLYAFVPG FIGDYKSDIT
VTITSGCSIE IDDLVFEPPR NGPTLWEIGI PDRSAREFYI PDPDPKYINK LFVNHPDKFR
QYGLWERYSD LYPNGDIVFT VGESDYKKDW FFAQVTRKRD EKTYIGTTWQ IKFKLDSVKQ
KEIYTLRVAL ASAAQAELQV RLNDSSTNTP LFSSGVIGKD NAIARHGIHG LHWLFNVNLQ
GNILVEGENT IYLTQANATS PFQGIMYDYI RLEGPPSHD
//
