ID   RHIE_DICD3              Reviewed;         578 AA.
AC   Q8RJP2; E0SBN8;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Rhamnogalacturonate lyase;
DE            Short=Rhamnogalacturonase;
DE            EC=4.2.2.23;
DE   Flags: Precursor;
GN   Name=rhiE; OrderedLocusNames=Dda3937_01465;
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP   CHARACTERIZATION.
RC   STRAIN=3937;
RX   PubMed=12591882; DOI=10.1128/jb.185.5.1642-1649.2003;
RA   Laatu M., Condemine G.;
RT   "Rhamnogalacturonate lyase RhiE is secreted by the out system in Erwinia
RT   chrysanthemi.";
RL   J. Bacteriol. 185:1642-1649(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=21217001; DOI=10.1128/jb.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- FUNCTION: Degrades the rhamnogalacturonan I (RG-I) backbone of pectin.
CC       Is required for the full virulence of E.chrysanthemi strain 3937 as it
CC       is involved in rotting of plant tissue.
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0.;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Via the type II out secretion
CC       pathway.
CC   -!- INDUCTION: By rhamnose.
CC   -!- MISCELLANEOUS: Contrary to other proteins secreted by the Out pathway,
CC       RhiE contains no disulfide bond.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Both Met-1 and Met-3 seem to be able to act as initiation
CC       codons. {ECO:0000305}.
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DR   EMBL; AJ438339; CAD27359.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADM97186.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RJP2; -.
DR   SMR; Q8RJP2; -.
DR   STRING; 198628.Dda3937_01465; -.
DR   CAZy; PL4; Polysaccharide Lyase Family 4.
DR   EnsemblBacteria; ADM97186; ADM97186; Dda3937_01465.
DR   KEGG; ddd:Dda3937_01465; -.
DR   eggNOG; ENOG502ZAF0; Bacteria.
DR   HOGENOM; CLU_021767_2_0_6; -.
DR   OMA; HGEGTPN; -.
DR   BRENDA; 4.2.2.23; 2141.
DR   Proteomes; UP000006859; Chromosome.
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; cd10316; RGL4_M; 1.
DR   Gene3D; 2.70.98.10; -; 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   Pfam; PF14683; CBM-like; 1.
DR   Pfam; PF14686; fn3_3; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Reference proteome; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:12591882"
FT   CHAIN           28..578
FT                   /note="Rhamnogalacturonate lyase"
FT                   /id="PRO_0000024914"
SQ   SEQUENCE   578 AA;  64978 MW;  82B177C96ABA1C47 CRC64;
     MHMNKPLQAW RTPLLTLIFV LPLTATGAVK LTLDGMNSTL DNGLLKVRFG ADGSAKEVWK
     GGTNLISRLS GAARDPDKNR SFYLDYYSGG VNEFVPERLE VIKQTPDQVH LAYIDDQNGK
     LRLEYHLIMT RDVSGLYSYV VAANTGSAPV TVSELRNVYR FDATRLDTLF NSIRRGTPLL
     YDELEQLPKV QDETWRLPDG SVYSKYDFAG YQRESRYWGV MGNGYGAWMV PASGEYYSGD
     ALKQELLVHQ DAIILNYLTG SHFGTPDMVA QPGFEKLYGP WLLYINQGND RELVADVSRR
     AEHERASWPY RWLDDARYPR QRATVSGRLR TEAPHATVVL NSSAENFDIQ TTGYLFSART
     NRDGRFSLSN VPPGEYRLSA YADGGTQIGL LAQQTVRVEG KKTRLGQIDA RQPAPLAWAI
     GQADRRADEF RFGDKPRQYR WQTEVPADLT FEIGKSRERK DWYYAQTQPG SWHILFNTRT
     PEQPYTLNIA IAAASNNGMT TPASSPQLAV KLNGQLLTTL KYDNDKSIYR GAMQSGRYHE
     AHIPLPAGAL QQGGNRITLE LLGGMVMYDA ITLTETPQ