ID   PORE_ZOBGA              Reviewed;         279 AA.
AC   D7GXG3;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Beta-porphyranase E;
DE            EC=3.2.1.178;
DE   Flags: Precursor;
GN   Name=porE; OrderedLocusNames=zobellia_3640;
OS   Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS   NCIMB 13871 / Dsij).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zobellia.
OX   NCBI_TaxID=63186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RX   PubMed=20376150; DOI=10.1038/nature08937;
RA   Hehemann J.H., Correc G., Barbeyron T., Helbert W., Czjzek M., Michel G.;
RT   "Transfer of carbohydrate-active enzymes from marine bacteria to Japanese
RT   gut microbiota.";
RL   Nature 464:908-912(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RG   Genoscope - CEA;
RT   "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4)
CC       linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-
CC       sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-
CC       sulfate-(1->3)-beta-D-galactose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-
CC         galactopyranose-6-sulfate linkages in porphyran.; EC=3.2.1.178;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; FQ073841; CBM41185.1; -; Genomic_DNA.
DR   EMBL; FP476056; CAZ97778.1; -; Genomic_DNA.
DR   RefSeq; WP_013994968.1; NC_015844.1.
DR   AlphaFoldDB; D7GXG3; -.
DR   SMR; D7GXG3; -.
DR   STRING; 63186.ZOBELLIA_3640; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   EnsemblBacteria; CAZ97778; CAZ97778; ZOBELLIA_3640.
DR   KEGG; zga:ZOBELLIA_3640; -.
DR   HOGENOM; CLU_053494_0_0_10; -.
DR   OMA; YGCWWVD; -.
DR   OrthoDB; 1046649at2; -.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0033916; F:beta-agarase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02178; GH16_beta_agarase; 1.
DR   InterPro; IPR016287; Beta_agarase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF001097; Agarase; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..279
FT                   /note="Beta-porphyranase E"
FT                   /id="PRO_0000422024"
FT   DOMAIN          19..277
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        141
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   ACT_SITE        146
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
SQ   SEQUENCE   279 AA;  31706 MW;  078C905ECE9D8F6B CRC64;
     MGNTMLLTLL LVVVAAYGQT PPPPEGFRWV KNESFSDEFD GEVLDTTKWY ARSPYWVNGR
     PPATFRAGSV SVKEGKLQIK NSVLDGDKKY NIAGGAVASV AKDALYGYYE ARMKASSISM
     SSTFWMKNKP DTKECPFEVQ ELDIVEVVGQ QKTGWDFRTN LKSNTHIFYT DCDGEKTVKS
     AGGTEAKIDP PADEAYHVYG CWWVDANTIK IYLDGEYQFT MNPSTHFRDT PFNKPMYMHM
     VTETYNWETP PTPEELADDT KNTTYYDWVR SYTLLPVDQ