BAGA_PHOPM
ID BAGA_PHOPM Reviewed; 316 AA.
AC B5CY73;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Beta-agarase;
DE EC=3.2.1.81;
DE AltName: Full=Glycosyl hydrolase 16 family protein A;
DE Short=GH16A;
DE Flags: Precursor;
GN ORFNames=BACPLE_01670;
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 FUNCTION, AND CATALYTIC 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 beta-1,4-linkages between beta-D-galactose and
CC alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a
CC random manner with retention of the anomeric-bond configuration,
CC producing beta-anomers that give rise progressively to alpha-anomers
CC when mutarotation takes place. {ECO:0000269|PubMed:23150581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose,
CC giving the tetramer as the predominant product.; EC=3.2.1.81;
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-agarases, which are active on agarose from marine
CC red algae of the genus Porphyra, are present in marine bacteria. They
CC are absent from metagenome data of gut bacteria, except from the genome
CC of the gut bacterium B.plebeius isolated from Japanese individuals.
CC Seaweeds make an important contribution to the diet in Japan and
CC Porphyra (nori) is the most important nutritional seaweed used to
CC prepare sushi, suggesting that seaweeds with associated marine bacteria
CC have been the route by which genes coding for beta-agarases have been
CC transferred in human gut B.plebeius genome (PubMed:20376150 and
CC 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; EDY95404.1; -; Genomic_DNA.
DR RefSeq; WP_007560915.1; NZ_DS990130.1.
DR AlphaFoldDB; B5CY73; -.
DR SMR; B5CY73; -.
DR STRING; 484018.BACPLE_01670; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; EDY95404; EDY95404; BACPLE_01670.
DR GeneID; 60971459; -.
DR eggNOG; COG2273; Bacteria.
DR HOGENOM; CLU_037753_0_0_10; -.
DR OrthoDB; 1046649at2; -.
DR Proteomes; UP000003452; Unassembled WGS sequence.
DR GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
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 PIRSF; PIRSF001097; Agarase; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..316
FT /note="Beta-agarase"
FT /id="PRO_0000422029"
FT DOMAIN 27..315
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 87..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 101..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
SQ SEQUENCE 316 AA; 36274 MW; 390E5D966B4018F2 CRC64;
MKRKLFTICL ASLQFACAAE NLNNKSYEWD IYPVPANAGD GMVWKLHPQS DDFNYIADEK
DKGKEFYAKW TDFYHNHWTG PAPTIWQRDH VSVSDGFLKI RASRPEDVPL KKVVSGPNTK
ELPGTYTGCI TSKTRVKYPV YVEAYAKLSN STMASDVWML SPDDTQEIDI IEAYGGDRDG
GGYGADRLHL SHHIFIRQPF KDYQPKDSGS WYKDDKGTLW RDDFHRVGVF WKDPFTLEYY
VDGELVRTIS GKDIIDPNNY TGGTGLVKDM DIIINMEDQS WRAVKGLSPT DEELKNVEDH
TFLVDWIRVY TLVPEE
