PORA_ZOBGA
ID PORA_ZOBGA Reviewed; 510 AA.
AC D7GXG0; D5MNX5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Beta-porphyranase A;
DE EC=3.2.1.178;
DE Flags: Precursor;
GN Name=porA; OrderedLocusNames=zobellia_2600;
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS)
RP OF 120-277 OF MUTANT MET-120; SER-139 AND ASP-148 IN COMPLEX WITH
RP ALPHA-L-GALACTOPYRANOSE-6-SULFATE, FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF LYS-120; GLU-139 AND ASN-148.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 18-277, AND FUNCTION.
RX PubMed=22778272; DOI=10.1074/jbc.m112.377184;
RA Hehemann J.H., Correc G., Thomas F., Bernard T., Barbeyron T., Jam M.,
RA Helbert W., Michel G., Czjzek M.;
RT "Biochemical and structural characterization of the complex agarolytic
RT enzyme system from the marine bacterium Zobellia galactanivorans.";
RL J. Biol. Chem. 287:30571-30584(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. Displays a strict
CC requirement for C6-sulfate in the -2 and +1-binding subsites.
CC {ECO:0000269|PubMed:20376150, ECO:0000269|PubMed:22778272}.
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:20376150};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ073838; CBM41182.1; -; Genomic_DNA.
DR EMBL; FP476056; CAZ96750.1; -; Genomic_DNA.
DR RefSeq; WP_013993946.1; NC_015844.1.
DR PDB; 3ILF; X-ray; 1.80 A; A=17-277.
DR PDB; 4ATE; X-ray; 1.10 A; A=18-277.
DR PDBsum; 3ILF; -.
DR PDBsum; 4ATE; -.
DR AlphaFoldDB; D7GXG0; -.
DR SMR; D7GXG0; -.
DR STRING; 63186.ZOBELLIA_2600; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAZ96750; CAZ96750; ZOBELLIA_2600.
DR KEGG; zga:ZOBELLIA_2600; -.
DR PATRIC; fig|63186.3.peg.2562; -.
DR HOGENOM; CLU_037753_0_0_10; -.
DR OrthoDB; 1046649at2; -.
DR BioCyc; MetaCyc:MON-16647; -.
DR BRENDA; 3.2.1.178; 7557.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR InterPro; IPR008999; Actin-crosslinking.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR026444; Secre_tail.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50405; SSF50405; 1.
DR TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..510
FT /note="Beta-porphyranase A"
FT /id="PRO_0000422020"
FT DOMAIN 18..275
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20376150"
FT MUTAGEN 120
FT /note="K->M: Abolishes beta-porphyranase activity; when
FT associated with S-139 and D-148."
FT /evidence="ECO:0000269|PubMed:20376150"
FT MUTAGEN 139
FT /note="E->S: Abolishes beta-porphyranase activity; when
FT associated with M-120 and D-148."
FT /evidence="ECO:0000269|PubMed:20376150"
FT MUTAGEN 148
FT /note="N->D: Abolishes beta-porphyranase activity; when
FT associated with M-120 and S-139."
FT /evidence="ECO:0000269|PubMed:20376150"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3ILF"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4ATE"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4ATE"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 135..148
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4ATE"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:4ATE"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:4ATE"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4ATE"
FT STRAND 260..273
FT /evidence="ECO:0007829|PDB:4ATE"
SQ SEQUENCE 510 AA; 57311 MW; 8ECE3DC51822FA7D CRC64;
MKKVLLFLIF LVSANLSAQL PSPTNGKKWE KVEQLSDEFN GNSIDTNKWY DYHPFWEGRA
PSNFKKGNAF VSDGFLNLRS TLRKEPSSVQ DPFKDIWVDA AAAVSKTKAQ PGYYYEARFK
ASSLSMTSSF WFRVGQFSEI DVIEHIGNPS KENRQDDLPY QYHVNTHYYG KHAGLQPLGT
EYKMPGRGRD NFYTYGFWWK SPNELLFYFN GKQVMRIVPR VPLDEELRMI FDTEVFPFAT
AGVANIGLPK PENLRDNSKN TMKVDWVRVY KLVDGTAAED SSDAPIGSYI SLKKTQGDGK
FVTGEKDGSQ LVARGSTVQS WEKFKVEKHP KGGITLKANS NGKYVQVQGS DINKPVRAAG
DFQGDWEQFE WKSKGNGLVA LKNVLTGKWL QAPWTENNAI IRPKGPVDNG WETFAWKKET
SPTASTALSA QLETKTVDGI RVYPSPASET LTIEGVEGEN GLRVFDSTGN PVLKKEGILG
RKERLNVSGL IKGNYLLRTG SGEQTWFQKN
