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Beta-porphyranase B (EC 3.2.1.178) (Glycosyl hydrolase 86 family protein B) (GH16B)

 PORB_BACPM              Reviewed;         321 AA.
B5CY92;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 1.
05-JUL-2017, entry version 37.
RecName: Full=Beta-porphyranase B;
EC=3.2.1.178;
AltName: Full=Glycosyl hydrolase 86 family protein B;
Short=GH16B;
Flags: Precursor;
ORFNames=BACPLE_01689;
Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=484018;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 17135 / JCM 12973 / M2;
Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
Liep D., Gordon J.;
"Draft genome sequence of Bacteroides plebeius (DSM 17135).";
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION.
STRAIN=DSM 17135 / JCM 12973 / M2;
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).
[3]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 21-321, FUNCTION, AND
CATALYTIC ACTIVITY.
STRAIN=DSM 17135 / JCM 12973 / M2;
PubMed=23150581; DOI=10.1073/pnas.1211002109;
Hehemann J.H., Kelly A.G., Pudlo N.A., Martens E.C., Boraston A.B.;
"Bacteria of the human gut microbiome catabolize red seaweed glycans
with carbohydrate-active enzyme updates from extrinsic microbes.";
Proc. Natl. Acad. Sci. U.S.A. 109:19786-19791(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. {ECO:0000269|PubMed:23150581}.
-!- CATALYTIC ACTIVITY: Hydrolysis of beta-D-galactopyranose-(1->4)-
alpha-L-galactopyranose-6-sulfate linkages in porphyran.
{ECO:0000269|PubMed:23150581}.
-!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
dietary polysaccharides through glycosidases that are absent in
the human genome. Beta-porphyranases, which are active on sulfated
polysaccharides from marine red algae of the genus Porphyra, are
present in marine bacteria. They are absent from metagenome data
of gut bacteria, except from the genome of the gut bacterium
B.plebeius isolated from Japanese individuals. Seaweeds make an
important contribution to the diet in Japan and Porphyra (nori) is
the most important nutritional seaweed used to prepare sushi,
suggesting that seaweeds with associated marine bacteria have been
the route by which genes coding for beta-porphyranases have been
transferred in human gut B.plebeius genome (PubMed:20376150 and
PubMed:23150581).
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A gut's tale - Issue
158 of March 2014;
URL="http://web.expasy.org/spotlight/back_issues/158/";
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EMBL; ABQC02000019; EDY95423.1; -; Genomic_DNA.
RefSeq; WP_007560951.1; NZ_DS990130.1.
PDB; 4AWD; X-ray; 2.40 A; A/B=21-321.
PDBsum; 4AWD; -.
ProteinModelPortal; B5CY92; -.
SMR; B5CY92; -.
STRING; 484018.BACPLE_01689; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
EnsemblBacteria; EDY95423; EDY95423; BACPLE_01689.
KEGG; ag:EDY95423; -.
eggNOG; ENOG4108ZIS; Bacteria.
eggNOG; ENOG4111NXQ; LUCA.
KO; K20830; -.
OrthoDB; POG091H03M1; -.
Proteomes; UP000003452; Unassembled WGS sequence.
GO; GO:0033916; F:beta-agarase activity; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
CDD; cd02178; GH16_beta_agarase; 1.
InterPro; IPR016287; Beta_agarase.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000757; GH16.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycosidase; Hydrolase; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 321 Beta-porphyranase B.
/FTId=PRO_0000422025.
DOMAIN 31 319 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
ACT_SITE 173 173 Nucleophile.
{ECO:0000250|UniProtKB:G0L322}.
ACT_SITE 178 178 Proton donor.
{ECO:0000250|UniProtKB:G0L322}.
BINDING 72 72 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 76 76 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 173 173 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 178 178 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 284 284 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
HELIX 27 31 {ECO:0000244|PDB:4AWD}.
HELIX 32 35 {ECO:0000244|PDB:4AWD}.
STRAND 43 47 {ECO:0000244|PDB:4AWD}.
HELIX 49 51 {ECO:0000244|PDB:4AWD}.
STRAND 57 59 {ECO:0000244|PDB:4AWD}.
TURN 62 64 {ECO:0000244|PDB:4AWD}.
STRAND 65 68 {ECO:0000244|PDB:4AWD}.
STRAND 70 72 {ECO:0000244|PDB:4AWD}.
STRAND 79 81 {ECO:0000244|PDB:4AWD}.
HELIX 83 85 {ECO:0000244|PDB:4AWD}.
STRAND 86 89 {ECO:0000244|PDB:4AWD}.
STRAND 92 96 {ECO:0000244|PDB:4AWD}.
STRAND 98 104 {ECO:0000244|PDB:4AWD}.
HELIX 106 108 {ECO:0000244|PDB:4AWD}.
STRAND 110 118 {ECO:0000244|PDB:4AWD}.
STRAND 120 124 {ECO:0000244|PDB:4AWD}.
STRAND 130 138 {ECO:0000244|PDB:4AWD}.
STRAND 141 144 {ECO:0000244|PDB:4AWD}.
STRAND 146 151 {ECO:0000244|PDB:4AWD}.
STRAND 155 163 {ECO:0000244|PDB:4AWD}.
STRAND 165 179 {ECO:0000244|PDB:4AWD}.
TURN 192 195 {ECO:0000244|PDB:4AWD}.
HELIX 196 198 {ECO:0000244|PDB:4AWD}.
STRAND 201 210 {ECO:0000244|PDB:4AWD}.
STRAND 216 218 {ECO:0000244|PDB:4AWD}.
STRAND 222 224 {ECO:0000244|PDB:4AWD}.
TURN 233 235 {ECO:0000244|PDB:4AWD}.
STRAND 238 246 {ECO:0000244|PDB:4AWD}.
STRAND 249 254 {ECO:0000244|PDB:4AWD}.
STRAND 257 262 {ECO:0000244|PDB:4AWD}.
STRAND 277 282 {ECO:0000244|PDB:4AWD}.
TURN 295 298 {ECO:0000244|PDB:4AWD}.
TURN 301 304 {ECO:0000244|PDB:4AWD}.
STRAND 305 318 {ECO:0000244|PDB:4AWD}.
SEQUENCE 321 AA; 37253 MW; 56EAC9B6C773F4FE CRC64;
MRKTVLYLSA ASLFLSSYTL KNDKEYSLAE EHIKNLPEAP EGYKWVVNED YTDEFNGKRL
NAAKWHAKSP YWTNGRPPAT FKAENVSVKK GCLRIINTVL SPTEGLDGKP GDKYRLAGGA
VASVKNQAHY GYYETRMKAS LTTMSSTFWL SNRPVMKEIM KGGKKIKTWS SQELDIIETM
GIIRSVNPDN PWNKTWNMQM NSNTHYWYQE QGGKRTDNTA KRSDVVSYMT DPSAEDFHTY
GCWWVDANTV KFYYDGKYMY TIKPTTKYTD TPFDRPMFIH IVTETYDWEK QVPTAEDLKD
KDKSTTYYDW VRAYKLVPIE E


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