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Database: UniProt
Entry: A0A1S4DP88_TOBAC
LinkDB: A0A1S4DP88_TOBAC
Original site: A0A1S4DP88_TOBAC 
ID   A0A1S4DP88_TOBAC        Unreviewed;       575 AA.
AC   A0A1S4DP88;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   Name=LOC107831685 {ECO:0000313|RefSeq:XP_016514954.1};
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_016514954.1};
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_016514954.1}
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_016514954.1; XM_016659468.1.
DR   AlphaFoldDB; A0A1S4DP88; -.
DR   STRING; 4097.A0A1S4DP88; -.
DR   PaxDb; 4097-A0A1S4DP88; -.
DR   GeneID; 107831685; -.
DR   KEGG; nta:107831685; -.
DR   OMA; DCAANET; -.
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_016514954.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          294..365
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          380..568
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   575 AA;  65950 MW;  AC7D39ABF31AE5B2 CRC64;
     MNSYLLDALF NVLICTTYKV ILERDDQIEL SFSRTWDVSL QDKLIPLNID KRFIMLKGSS
     GFYSYAIYEH LEVWPGFNLD ETRIAFKLRK DKFHYMAMAD NRQRYMPLPD DRLPDRGQPL
     AYPEAVLLVN PVEPELKGEV DDKYQYSSED KDLKVHGWIC MDPPLGFWII IPSDEFRSGG
     PLKQNLTSHV GPTALSVFLS AHYAGEDLVP KFGEGESWKK IFGPVFIYLN SVTGGKDPLI
     LWEDAKEQML VEVQSWPYSF PASEDFPSSS QRGNISGRLL VQDRYFKDDK IYASGAYVGL
     APPGEAGSWQ RECKDYQFWT KADEEGYYVI SDIRAGDYNL YAFVPGFIGD YKSDTKVTIT
     SGCSIEMDDL VFEPPRNGPT LWEIGIPDRS AREFYIPDPD PKYINKLFVN HPDKFRQYGL
     WERYTDLYPN GDIVFTIGES DYKKDWFFAQ VTRKKDEKTY TGTTWQIKFK LDSVNRNETY
     SLRLALASVA QAELQVRIND SSMNTPLFSS GLIGKDNAIA RHGIHGLYWL FNVNLQGDML
     VEGENTIYLT QANATSPFQG IMYDYIRLEA PPSHD
//
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