ID   PORC_ZOBGA              Reviewed;         355 AA.
AC   D7GXG1;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Beta-porphyranase C;
DE            EC=3.2.1.178;
DE   Flags: Precursor;
GN   Name=porC; OrderedLocusNames=zobellia_3376;
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: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; FQ073839; CBM41183.1; -; Genomic_DNA.
DR   EMBL; FP476056; CAZ97514.1; -; Genomic_DNA.
DR   RefSeq; WP_013994707.1; NC_015844.1.
DR   AlphaFoldDB; D7GXG1; -.
DR   SMR; D7GXG1; -.
DR   STRING; 63186.ZOBELLIA_3376; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   EnsemblBacteria; CAZ97514; CAZ97514; ZOBELLIA_3376.
DR   KEGG; zga:ZOBELLIA_3376; -.
DR   PATRIC; fig|63186.3.peg.3293; -.
DR   HOGENOM; CLU_053494_0_0_10; -.
DR   OMA; FHYNTHR; -.
DR   OrthoDB; 1046649at2; -.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..355
FT                   /note="Beta-porphyranase C"
FT                   /id="PRO_0000422022"
FT   DOMAIN          71..355
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          22..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        208
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:G0L322"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   355 AA;  40646 MW;  2934527FF72B5011 CRC64;
     MIKTLKRIPL VFLIAIMACS NSGDNGKDKV EEQEQAQEQG EKKGQGEERD KEDGIDGLQP
     TFLADQDPKP DDKKWIKVEG VSDEFNDSEL DLTKWSPTPE FIWNGQDRGW YGGSRSLFEA
     DNVSVGNGFL RIEGEKFDSP KYSPKDNTDT PPQRRYGGAY VYGKTLAEPG YYIEARMRAS
     KTAMSAAFWL KTETKPCGEN LNDGENLEID IQECVGVFTG ELGDEWTKDD WAVNANWDRI
     FHYNTHRHNS PCNNIGDRQT KGGKANFDKK NSDEFHIYAA YWHADGSKID FYIDGELEKS
     ITPVIPFKGA LRLIMSSNFY DWIEETSAED MGFNRPLEDR YTQFDWVRVW QLEDL