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Database: UniProt
Entry: A0A1M5V2X0_9VIBR
LinkDB: A0A1M5V2X0_9VIBR
Original site: A0A1M5V2X0_9VIBR 
ID   A0A1M5V2X0_9VIBR        Unreviewed;       555 AA.
AC   A0A1M5V2X0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE            EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN   ORFNames=VA7868_00241 {ECO:0000313|EMBL:SHH69303.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHH69303.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHH69303.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHH69303.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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   EMBL; FQXZ01000005; SHH69303.1; -; Genomic_DNA.
DR   RefSeq; WP_073602035.1; NZ_FQXZ01000005.1.
DR   AlphaFoldDB; A0A1M5V2X0; -.
DR   STRING; 1216006.VA7868_00241; -.
DR   OrthoDB; 7169863at2; -.
DR   Proteomes; UP000184608; 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   CDD; cd10316; RGL4_M; 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:UP000184608};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..555
FT                   /note="rhamnogalacturonan endolyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012206434"
FT   DOMAIN          26..288
FT                   /note="Rhamnogalacturonase B N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09284"
FT   DOMAIN          295..369
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14686"
FT   DOMAIN          385..553
FT                   /note="Rhamnogalacturonan lyase"
FT                   /evidence="ECO:0000259|Pfam:PF14683"
SQ   SEQUENCE   555 AA;  61013 MW;  AB9221A74DC11CC5 CRC64;
     MKYLLTTQGL ICGLGLAFAT GANASFSLKS DSNFYTVDTN AGVVFSVRRT DNNVSTQSAG
     DIASLKINGK EFQNQSRGSQ INAGFDWLYK NTSDVKVSAT KIGSDYIKVT VKAGKLTHYY
     MARKGYPNIY MATYFTGEPD VHNHVRYILR MKRSQLPYGP EPSDISKTTS TVEASDIFAL
     SNGETRSKHY SNQRLKDWKY IGATGNNVGV WVVRDGMEGS SGGPFYRSLL NQGTAGDQEI
     TYIINYGQAQ TESFRPGILN HYTLVVNKGQ APSTDIDTSW FSKMGLTGYV ADSKRGRVSG
     VGINNRNTDY DYTVGFANSK AQYWADANIA SGYFSTPYML PGTYDMTIYK NELAVQKQQV
     TVTAGNTTVL HTISIQDDPG NDGVIWRIGK WDGSPQEFMN GSKLTTMHPS DVRMSKWDGS
     NFIVGSSSTN SFPAYIWKDV NNNHVIYFRL NASQRAKAHT LRFGITDAMA GGRPQIKVND
     WTSKIPSASS QPKTRSLTTG SYRGNNTTFE YSIPASAWKN SDSDWNSLVI NVVSGTTSSG
     YLSPAISVDA IDLLK
//
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