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Beta-porphyranase A (EC 3.2.1.178)

 PORA_ZOBGA              Reviewed;         510 AA.
D7GXG0; D5MNX5;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 1.
07-JUN-2017, entry version 42.
RecName: Full=Beta-porphyranase A;
EC=3.2.1.178;
Flags: Precursor;
Name=porA; OrderedLocusNames=zobellia_2600;
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
NCIMB 13871 / Dsij).
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Zobellia.
NCBI_TaxID=63186;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.80
ANGSTROMS) OF 120-277 OF MUTANT MET-120; SER-139 AND ASP-148 IN
COMPLEX WITH ALPHA-L-GALACTOPYRANOSE-6-SULFATE, FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF LYS-120; GLU-139 AND ASN-148.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
Genoscope - CEA;
"Complete genome sequence of Zobellia galactanivorans Dsij.";
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 18-277, AND FUNCTION.
PubMed=22778272; DOI=10.1074/jbc.M112.377184;
Hehemann J.H., Correc G., Thomas F., Bernard T., Barbeyron T., Jam M.,
Helbert W., Michel G., Czjzek M.;
"Biochemical and structural characterization of the complex agarolytic
enzyme system from the marine bacterium Zobellia galactanivorans.";
J. Biol. Chem. 287:30571-30584(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. Displays a strict requirement for C6-sulfate in the -2
and +1-binding subsites. {ECO:0000269|PubMed:20376150,
ECO:0000269|PubMed:22778272}.
-!- CATALYTIC ACTIVITY: Hydrolysis of beta-D-galactopyranose-(1->4)-
alpha-L-galactopyranose-6-sulfate linkages in porphyran.
{ECO:0000269|PubMed:20376150}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
{ECO:0000305}.
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EMBL; FQ073838; CBM41182.1; -; Genomic_DNA.
EMBL; FP476056; CAZ96750.1; -; Genomic_DNA.
RefSeq; WP_013993946.1; NC_015844.1.
PDB; 3ILF; X-ray; 1.80 A; A=17-277.
PDB; 4ATE; X-ray; 1.10 A; A=18-277.
PDBsum; 3ILF; -.
PDBsum; 4ATE; -.
ProteinModelPortal; D7GXG0; -.
SMR; D7GXG0; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
EnsemblBacteria; CAZ96750; CAZ96750; ZOBELLIA_2600.
KEGG; zga:ZOBELLIA_2600; -.
PATRIC; fig|63186.3.peg.2562; -.
KO; K20830; -.
BRENDA; 3.2.1.178; 7557.
Proteomes; UP000008898; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
GO; GO:0008152; P:metabolic process; IDA:UniProtKB.
InterPro; IPR008999; Actin_cross-linking.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000757; GH16.
InterPro; IPR026444; Secre_tail.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50405; SSF50405; 1.
TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycosidase; Hydrolase; Periplasm;
Reference proteome; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 510 Beta-porphyranase A.
/FTId=PRO_0000422020.
DOMAIN 18 275 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
ACT_SITE 139 139 Nucleophile.
{ECO:0000250|UniProtKB:G0L322}.
ACT_SITE 144 144 Proton donor.
{ECO:0000250|UniProtKB:G0L322}.
BINDING 56 56 Substrate. {ECO:0000269|PubMed:20376150}.
BINDING 59 59 Substrate. {ECO:0000269|PubMed:20376150}.
BINDING 134 134 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:20376150}.
BINDING 139 139 Substrate. {ECO:0000269|PubMed:20376150}.
BINDING 144 144 Substrate. {ECO:0000269|PubMed:20376150}.
BINDING 234 234 Substrate. {ECO:0000269|PubMed:20376150}.
MUTAGEN 120 120 K->M: Abolishes beta-porphyranase
activity; when associated with S-139 and
D-148. {ECO:0000269|PubMed:20376150}.
MUTAGEN 139 139 E->S: Abolishes beta-porphyranase
activity; when associated with M-120 and
D-148. {ECO:0000269|PubMed:20376150}.
MUTAGEN 148 148 N->D: Abolishes beta-porphyranase
activity; when associated with M-120 and
S-139. {ECO:0000269|PubMed:20376150}.
HELIX 24 26 {ECO:0000244|PDB:3ILF}.
STRAND 28 31 {ECO:0000244|PDB:4ATE}.
HELIX 33 35 {ECO:0000244|PDB:4ATE}.
STRAND 41 43 {ECO:0000244|PDB:4ATE}.
TURN 46 48 {ECO:0000244|PDB:4ATE}.
STRAND 49 52 {ECO:0000244|PDB:4ATE}.
STRAND 62 64 {ECO:0000244|PDB:4ATE}.
STRAND 68 72 {ECO:0000244|PDB:4ATE}.
STRAND 75 79 {ECO:0000244|PDB:4ATE}.
STRAND 81 84 {ECO:0000244|PDB:4ATE}.
HELIX 86 88 {ECO:0000244|PDB:4ATE}.
TURN 92 94 {ECO:0000244|PDB:4ATE}.
STRAND 98 100 {ECO:0000244|PDB:4ATE}.
STRAND 102 107 {ECO:0000244|PDB:4ATE}.
STRAND 114 120 {ECO:0000244|PDB:4ATE}.
STRAND 123 133 {ECO:0000244|PDB:4ATE}.
STRAND 135 148 {ECO:0000244|PDB:4ATE}.
HELIX 152 154 {ECO:0000244|PDB:4ATE}.
TURN 155 157 {ECO:0000244|PDB:4ATE}.
HELIX 158 160 {ECO:0000244|PDB:4ATE}.
STRAND 161 168 {ECO:0000244|PDB:4ATE}.
HELIX 170 172 {ECO:0000244|PDB:4ATE}.
STRAND 180 183 {ECO:0000244|PDB:4ATE}.
HELIX 188 190 {ECO:0000244|PDB:4ATE}.
STRAND 193 201 {ECO:0000244|PDB:4ATE}.
STRAND 204 209 {ECO:0000244|PDB:4ATE}.
STRAND 212 217 {ECO:0000244|PDB:4ATE}.
STRAND 227 232 {ECO:0000244|PDB:4ATE}.
STRAND 237 240 {ECO:0000244|PDB:4ATE}.
HELIX 251 254 {ECO:0000244|PDB:4ATE}.
TURN 257 259 {ECO:0000244|PDB:4ATE}.
STRAND 260 273 {ECO:0000244|PDB:4ATE}.
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


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