ID   PORD_ZOBGA              Reviewed;         427 AA.
AC   D7GXG2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Beta-porphyranase D;
DE            EC=3.2.1.178;
DE   Flags: Precursor;
GN   Name=porD; OrderedLocusNames=zobellia_3628;
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; FQ073840; CBM41184.1; -; Genomic_DNA.
DR   EMBL; FP476056; CAZ97766.1; -; Genomic_DNA.
DR   RefSeq; WP_013994956.1; NC_015844.1.
DR   AlphaFoldDB; D7GXG2; -.
DR   SMR; D7GXG2; -.
DR   STRING; 63186.ZOBELLIA_3628; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PRIDE; D7GXG2; -.
DR   EnsemblBacteria; CAZ97766; CAZ97766; ZOBELLIA_3628.
DR   KEGG; zga:ZOBELLIA_3628; -.
DR   HOGENOM; CLU_642431_0_0_10; -.
DR   OrthoDB; 1046649at2; -.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..427
FT                   /note="Beta-porphyranase D"
FT                   /id="PRO_0000422023"
FT   DOMAIN          32..308
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          23..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
SQ   SEQUENCE   427 AA;  49106 MW;  BA2C91C896ECFC6E CRC64;
     MILKQAILTL VLVNANLFAQ EPPKTYSSTD KETRQGPPKP PMGKRWVLNP DFSDEFNGTE
     LDTTKWLDHH PTWIGRAPGL FMSSQVSVGD GFLKMEGKKL EKDTIVHAYG KDITFNIAGA
     AVVSKKATKF GYYECRVKAA ATTMSTTFWF SSSNNFKGPK DCDRYGLEWD IHESIGREGD
     FNGSYFASGM HSNAHFWYTD CNGKKYDHRA PQVKFEDAKL TSEDFNVYGG WWRDESTASY
     YYNNRPPKHQ KFYDKVKKKP FDQPMYMRLV NETYPFPWIE LPNAEELSDP SKNTVYYDWV
     RAYRLVDVND PNSEVEKDPT LKLYHENVTF PSATIEHKRS KSLEIPLSYQ ANEDREIAFI
     LFDNEGKKIK EAILTAYAGY ANLEYTLQLD QKLPLGSPYK LSAHIRPLKG NKKNSLDEST
     VYIHLTK