PORB_PHOPM
ID PORB_PHOPM Reviewed; 321 AA.
AC B5CY92;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Beta-porphyranase B;
DE EC=3.2.1.178;
DE AltName: Full=Glycosyl hydrolase 86 family protein B;
DE Short=GH16B;
DE Flags: Precursor;
GN ORFNames=BACPLE_01689;
OS Phocaeicola plebeius (strain DSM 17135 / JCM 12973 / M2) (Bacteroides
OS plebeius).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=484018;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17135 / JCM 12973 / M2;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides plebeius (DSM 17135).";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RC STRAIN=DSM 17135 / JCM 12973 / M2;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 21-321, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=DSM 17135 / JCM 12973 / M2;
RX PubMed=23150581; DOI=10.1073/pnas.1211002109;
RA Hehemann J.H., Kelly A.G., Pudlo N.A., Martens E.C., Boraston A.B.;
RT "Bacteria of the human gut microbiome catabolize red seaweed glycans with
RT carbohydrate-active enzyme updates from extrinsic microbes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19786-19791(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.
CC {ECO:0000269|PubMed:23150581}.
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:23150581};
CC -!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
CC dietary polysaccharides through glycosidases that are absent in the
CC human genome. Beta-porphyranases, which are active on sulfated
CC polysaccharides from marine red algae of the genus Porphyra, are
CC present in marine bacteria. They are absent from metagenome data of gut
CC bacteria, except from the genome of the gut bacterium B.plebeius
CC isolated from Japanese individuals. Seaweeds make an important
CC contribution to the diet in Japan and Porphyra (nori) is the most
CC important nutritional seaweed used to prepare sushi, suggesting that
CC seaweeds with associated marine bacteria have been the route by which
CC genes coding for beta-porphyranases have been transferred in human gut
CC B.plebeius genome (PubMed:20376150 and PubMed:23150581).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A gut's tale - Issue 158 of
CC March 2014;
CC URL="https://web.expasy.org/spotlight/back_issues/158/";
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DR EMBL; ABQC02000019; EDY95423.1; -; Genomic_DNA.
DR RefSeq; WP_007560951.1; NZ_DS990130.1.
DR PDB; 4AWD; X-ray; 2.40 A; A/B=21-321.
DR PDBsum; 4AWD; -.
DR AlphaFoldDB; B5CY92; -.
DR SMR; B5CY92; -.
DR STRING; 484018.BACPLE_01689; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; EDY95423; EDY95423; BACPLE_01689.
DR GeneID; 60971476; -.
DR KEGG; ag:EDY95423; -.
DR eggNOG; COG2273; Bacteria.
DR HOGENOM; CLU_053494_0_0_10; -.
DR OrthoDB; 1046649at2; -.
DR BRENDA; 3.2.1.178; 14050.
DR Proteomes; UP000003452; Unassembled WGS sequence.
DR GO; GO:0033916; F:beta-agarase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02178; GH16_beta_agarase; 1.
DR InterPro; IPR016287; Beta_agarase.
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; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..321
FT /note="Beta-porphyranase B"
FT /id="PRO_0000422025"
FT DOMAIN 31..319
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:4AWD"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:4AWD"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4AWD"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4AWD"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4AWD"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 165..179
FT /evidence="ECO:0007829|PDB:4AWD"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:4AWD"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4AWD"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4AWD"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:4AWD"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:4AWD"
FT STRAND 305..318
FT /evidence="ECO:0007829|PDB:4AWD"
SQ 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