PORA_PHOPM
ID PORA_PHOPM Reviewed; 728 AA.
AC B5CY96;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Beta-porphyranase A;
DE EC=3.2.1.178;
DE AltName: Full=Glycosyl hydrolase 86 family protein A;
DE Short=GH86A;
DE Flags: Precursor;
GN ORFNames=BACPLE_01693;
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 X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 30-598 IN COMPLEX WITH
RP PORPHYRAN-AGAROSE-OLIGOSACCHARIDE, 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 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:23150581). {ECO:0000305|PubMed:23150581}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 86 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; EDY95427.1; -; Genomic_DNA.
DR RefSeq; WP_007560960.1; NZ_DS990130.1.
DR PDB; 4AW7; X-ray; 1.33 A; A=30-598.
DR PDBsum; 4AW7; -.
DR AlphaFoldDB; B5CY96; -.
DR SMR; B5CY96; -.
DR STRING; 484018.BACPLE_01693; -.
DR CAZy; GH86; Glycoside Hydrolase Family 86.
DR EnsemblBacteria; EDY95427; EDY95427; BACPLE_01693.
DR GeneID; 60971479; -.
DR eggNOG; COG3401; Bacteria.
DR HOGENOM; CLU_019012_1_0_10; -.
DR OrthoDB; 66128at2; -.
DR BRENDA; 3.2.1.178; 14050.
DR Proteomes; UP000003452; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR041224; BPA_C.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR040527; Porphyrn_cat_1.
DR Pfam; PF18040; BPA_C; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF18206; Porphyrn_cat_1; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..728
FT /note="Beta-porphyranase A"
FT /id="PRO_0000422034"
FT DOMAIN 599..701
FT /note="CBM-cenC"
FT BINDING 53
FT /ligand="substrate"
FT BINDING 77..78
FT /ligand="substrate"
FT BINDING 87
FT /ligand="substrate"
FT BINDING 114
FT /ligand="substrate"
FT BINDING 151..152
FT /ligand="substrate"
FT BINDING 156
FT /ligand="substrate"
FT BINDING 237
FT /ligand="substrate"
FT BINDING 324
FT /ligand="substrate"
FT BINDING 331
FT /ligand="substrate"
FT BINDING 342
FT /ligand="substrate"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 188..193
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 206..211
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 275..284
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 294..299
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 419..424
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 425..436
FT /evidence="ECO:0007829|PDB:4AW7"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 440..450
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 461..469
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 498..505
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 509..521
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 529..532
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 551..562
FT /evidence="ECO:0007829|PDB:4AW7"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 569..577
FT /evidence="ECO:0007829|PDB:4AW7"
FT STRAND 583..596
FT /evidence="ECO:0007829|PDB:4AW7"
SQ SEQUENCE 728 AA; 81281 MW; 192BD9484B946F0E CRC64;
MSYKYIFLLS AFTLGVPPGI YCQGRNEVVV DYNTRRFLSG VSELDRSKYF NIHSTSDDDK
DVGKFLADYQ VGLGRKFWGP YSYAYNKTHE VGKYPQMKPY SGNISVKRYI ATEHPYVQHI
QGGIDVQAAG AWSAEYYSNS ELVPEFFEPL NEPFVHANDA GFTVQGQAMR ELMVDFYASI
GKHIHNNPRL NGKMKVIGYA AAYPAWEDGN FNYWNTRMKM FIDRAGAYMD GFSVHLYDGI
NVTGTDTKRS GSNSEAVLDM VEAYSYIKFG HVKPLAISEF GGIDNSKPDD SYDDISSVRS
VSSFNHFLFN LMERQDNLFI SIPFVSDKAE WHITAANNYT SYSAALFIPD NPQNLKNTTW
RLNDKKYFFE LWKNVKGERV DITSSNPDIQ VQAFKDGGRL YIALDNLDDN PQTVYLNNKN
SWKDVSNVTK RSLYVNYNAG IEYTEQNVPS MPESISIVPN QTIVLVADVS SSAFTNSIIR
NKYYSSEYLK PISAGSSLSF PFTGIESGSG RASLRMSIGR PVSASKKPVV KINGTAVSVP
DNWKGYGQSN RNIFFGMIEV PFDIQLLKNG DNNVDITFSD GGGHVSSMIL QVEKYTVSTL
QNGTFSEGLS AWQPLGNYGT VCVQTDNAGN NVACISGHAG LMQRVDMESG RTYRFSADVK
TEGACKLKVM LQDMSTGTVY TEEFSSPGNY KAVSFDFNST VKKVVCAIVC ERQNDAAWID
NIVLLPQN
