PORB_ZOBGA
ID PORB_ZOBGA Reviewed; 293 AA.
AC D7GXF9; D5MNX6;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Beta-porphyranase B;
DE EC=3.2.1.178;
DE Flags: Precursor;
GN Name=porB; OrderedLocusNames=zobellia_1017;
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], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS)
RP OF 46-293, FUNCTION, AND CATALYTIC ACTIVITY.
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.
RN [3]
RP FUNCTION.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RX PubMed=22778272; DOI=10.1074/jbc.m112.377184;
RA Hehemann J.H., Correc G., Thomas F., Bernard T., Barbeyron T., Jam M.,
RA Helbert W., Michel G., Czjzek M.;
RT "Biochemical and structural characterization of the complex agarolytic
RT enzyme system from the marine bacterium Zobellia galactanivorans.";
RL J. Biol. Chem. 287:30571-30584(2012).
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. Some longer oligosaccharides of even
CC number of residues are also observed. Inactive on the non-sulfated
CC agarose portion of the porphyran backbone. In contrast to PorA,
CC tolerates the presence of 3-6-anhydro-L-galactose in subsite -2.
CC {ECO:0000269|PubMed:20376150, ECO:0000269|PubMed:22778272}.
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 Evidence={ECO:0000269|PubMed:20376150};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ073837; CBM41181.1; -; Genomic_DNA.
DR EMBL; FP476056; CAZ95074.1; -; Genomic_DNA.
DR RefSeq; WP_013992386.1; NC_015844.1.
DR PDB; 3JUU; X-ray; 1.80 A; A/B=22-293.
DR PDBsum; 3JUU; -.
DR AlphaFoldDB; D7GXF9; -.
DR SMR; D7GXF9; -.
DR STRING; 63186.ZOBELLIA_1017; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAZ95074; CAZ95074; ZOBELLIA_1017.
DR KEGG; zga:ZOBELLIA_1017; -.
DR PATRIC; fig|63186.3.peg.1000; -.
DR HOGENOM; CLU_053494_0_0_10; -.
DR OMA; MNSNTHS; -.
DR OrthoDB; 1046649at2; -.
DR BioCyc; MetaCyc:MON-16646; -.
DR BRENDA; 3.2.1.178; 7557.
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; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..293
FT /note="Beta-porphyranase B"
FT /id="PRO_0000422021"
FT DOMAIN 38..291
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3JUU"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 103..116
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 153..165
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3JUU"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3JUU"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3JUU"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:3JUU"
SQ SEQUENCE 293 AA; 33622 MW; 6A713EF91259F3C5 CRC64;
MKLSNQFLIT ITLLITSITF AQEAPHFKPG EDPRQPHQEW KLIENMSDEF EGKKIDEKKW
QISGQGWIGR APGLFLAENI SLNNGSLQIT TTMLPEPIVK NNKTYTHGGG YVGSRNGMTY
GYYECEMKAN KTFMSSTFWL INEGKDRLGC DKRTTELDIQ ESVGQITNDA DWMKYFDQTM
NSNTHSRNIP EGCEYEKGSS KGKAELGGKA YEDFHVYGVW WKSKDEIIFF LDGKMQSKVT
PPADFDIEMY LRMVVETYDW NPVPKDGGMT GSKEDRTTTY NWVRSWQLVD SKN
