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Beta-porphyranase B (EC 3.2.1.178)

 PORB_ZOBGA              Reviewed;         293 AA.
D7GXF9; D5MNX6;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 1.
22-NOV-2017, entry version 42.
RecName: Full=Beta-porphyranase B;
EC=3.2.1.178;
Flags: Precursor;
Name=porB; OrderedLocusNames=zobellia_1017;
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
NCIMB 13871 / Dsij).
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Zobellia.
NCBI_TaxID=63186;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.80
ANGSTROMS) OF 46-293, FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
PubMed=20376150; DOI=10.1038/nature08937;
Hehemann J.H., Correc G., Barbeyron T., Helbert W., Czjzek M.,
Michel G.;
"Transfer of carbohydrate-active enzymes from marine bacteria to
Japanese gut microbiota.";
Nature 464:908-912(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
Genoscope - CEA;
"Complete genome sequence of Zobellia galactanivorans Dsij.";
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
PubMed=22778272; DOI=10.1074/jbc.M112.377184;
Hehemann J.H., Correc G., Thomas F., Bernard T., Barbeyron T., Jam M.,
Helbert W., Michel G., Czjzek M.;
"Biochemical and structural characterization of the complex agarolytic
enzyme system from the marine bacterium Zobellia galactanivorans.";
J. Biol. Chem. 287:30571-30584(2012).
-!- FUNCTION: Cleaves the sulfated polysaccharide porphyran at the
(1->4) linkages between beta-D-galactopyranose and alpha-L-
galactopyranose-6-sulfate, forming mostly the disaccharide alpha-
L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer
oligosaccharides of even number of residues are also observed.
Inactive on the non-sulfated agarose portion of the porphyran
backbone. In contrast to PorA, tolerates the presence of 3-6-
anhydro-L-galactose in subsite -2. {ECO:0000269|PubMed:20376150,
ECO:0000269|PubMed:22778272}.
-!- CATALYTIC ACTIVITY: Hydrolysis of beta-D-galactopyranose-(1->4)-
alpha-L-galactopyranose-6-sulfate linkages in porphyran.
{ECO:0000269|PubMed:20376150}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
{ECO:0000305}.
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EMBL; FQ073837; CBM41181.1; -; Genomic_DNA.
EMBL; FP476056; CAZ95074.1; -; Genomic_DNA.
RefSeq; WP_013992386.1; NC_015844.1.
PDB; 3JUU; X-ray; 1.80 A; A/B=22-293.
PDBsum; 3JUU; -.
ProteinModelPortal; D7GXF9; -.
SMR; D7GXF9; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
EnsemblBacteria; CAZ95074; CAZ95074; ZOBELLIA_1017.
KEGG; zga:ZOBELLIA_1017; -.
PATRIC; fig|63186.3.peg.1000; -.
KO; K20830; -.
OMA; RNIPEGC; -.
BRENDA; 3.2.1.178; 7557.
Proteomes; UP000008898; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
GO; GO:0008152; P:metabolic process; IDA:UniProtKB.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000757; GH16.
Pfam; PF00722; Glyco_hydro_16; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycosidase; Hydrolase; Periplasm;
Reference proteome; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 293 Beta-porphyranase B.
/FTId=PRO_0000422021.
DOMAIN 38 291 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
ACT_SITE 156 156 Nucleophile.
{ECO:0000250|UniProtKB:G0L322}.
ACT_SITE 161 161 Proton donor.
{ECO:0000250|UniProtKB:G0L322}.
BINDING 67 67 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 70 70 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 156 156 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 161 161 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 256 256 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
STRAND 39 42 {ECO:0000244|PDB:3JUU}.
HELIX 44 46 {ECO:0000244|PDB:3JUU}.
STRAND 52 54 {ECO:0000244|PDB:3JUU}.
TURN 57 59 {ECO:0000244|PDB:3JUU}.
STRAND 73 75 {ECO:0000244|PDB:3JUU}.
HELIX 77 79 {ECO:0000244|PDB:3JUU}.
STRAND 80 83 {ECO:0000244|PDB:3JUU}.
STRAND 86 90 {ECO:0000244|PDB:3JUU}.
STRAND 92 100 {ECO:0000244|PDB:3JUU}.
STRAND 103 116 {ECO:0000244|PDB:3JUU}.
STRAND 118 128 {ECO:0000244|PDB:3JUU}.
STRAND 131 141 {ECO:0000244|PDB:3JUU}.
HELIX 144 146 {ECO:0000244|PDB:3JUU}.
HELIX 149 152 {ECO:0000244|PDB:3JUU}.
STRAND 153 165 {ECO:0000244|PDB:3JUU}.
HELIX 171 173 {ECO:0000244|PDB:3JUU}.
HELIX 176 178 {ECO:0000244|PDB:3JUU}.
STRAND 179 187 {ECO:0000244|PDB:3JUU}.
STRAND 202 205 {ECO:0000244|PDB:3JUU}.
TURN 210 212 {ECO:0000244|PDB:3JUU}.
STRAND 215 223 {ECO:0000244|PDB:3JUU}.
STRAND 226 231 {ECO:0000244|PDB:3JUU}.
STRAND 234 239 {ECO:0000244|PDB:3JUU}.
STRAND 249 255 {ECO:0000244|PDB:3JUU}.
HELIX 273 276 {ECO:0000244|PDB:3JUU}.
STRAND 277 289 {ECO:0000244|PDB:3JUU}.
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


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