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Beta-agarase A (EC 3.2.1.81) [Cleaved into: Beta-agarase A catalytic chain (AgaAc)]

 AGAA_ZOBGA              Reviewed;         539 AA.
G0L322; Q9RGX9;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
05-JUL-2017, entry version 36.
RecName: Full=Beta-agarase A;
EC=3.2.1.81;
Contains:
RecName: Full=Beta-agarase A catalytic chain;
Short=AgaAc;
Flags: Precursor;
Name=agaA; OrderedLocusNames=zobellia_4203;
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], PROTEIN SEQUENCE OF 116-125,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND SUBCELLULAR LOCATION.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
PubMed=15456406; DOI=10.1042/BJ20041044;
Jam M., Flament D., Allouch J., Potin P., Thion L., Kloareg B.,
Czjzek M., Helbert W., Michel G., Barbeyron T.;
"The endo-beta-agarases AgaA and AgaB from the marine bacterium
Zobellia galactanivorans: two paralogue enzymes with different
molecular organizations and catalytic behaviours.";
Biochem. J. 385:703-713(2005).
[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]
INDUCTION.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
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).
[4]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 20-295, AND ACTIVE SITE.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
PubMed=12970344; DOI=10.1074/jbc.M308313200;
Allouch J., Jam M., Helbert W., Barbeyron T., Kloareg B.,
Henrissat B., Czjzek M.;
"The three-dimensional structures of two beta-agarases.";
J. Biol. Chem. 278:47171-47180(2003).
[5]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 20-290 OF MUTANT SER-147 IN
COMPLEX WITH GALACTOSE, AND MUTAGENESIS OF GLU-147.
STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
PubMed=15062085; DOI=10.1016/j.str.2004.02.020;
Allouch J., Helbert W., Henrissat B., Czjzek M.;
"Parallel substrate binding sites in a beta-agarase suggest a novel
mode of action on double-helical agarose.";
Structure 12:623-632(2004).
-!- FUNCTION: Cleaves the beta-1,4-linkages between beta-D-galactose
and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves
agarose in a random manner with retention of the anomeric-bond
configuration, producing beta-anomers that give rise progressively
to alpha-anomers when mutarotation takes place.
{ECO:0000269|PubMed:15456406}.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-galactosidic
linkages in agarose, giving the tetramer as the predominant
product. {ECO:0000269|PubMed:15456406}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 mM for agarose {ECO:0000269|PubMed:15456406};
Note=kcat is 150 sec(-1).;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15062085,
ECO:0000269|PubMed:15456406}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}.
-!- INDUCTION: When cells are grown with the low sulfated agar.
{ECO:0000269|PubMed:22778272}.
-!- PTM: Proteolytically cleaved into mature beta-agarase A catalytic
chain (AgaAc). {ECO:0000269|PubMed:15456406}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF098954; AAF21820.1; -; Genomic_DNA.
EMBL; FP476056; CAZ98338.1; -; Genomic_DNA.
PDB; 1O4Y; X-ray; 1.48 A; A=20-295.
PDB; 1URX; X-ray; 1.70 A; A=20-290.
PDBsum; 1O4Y; -.
PDBsum; 1URX; -.
SMR; G0L322; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
EnsemblBacteria; CAZ98338; CAZ98338; ZOBELLIA_4203.
KEGG; zga:ZOBELLIA_4203; -.
KO; K01219; -.
BRENDA; 3.2.1.81; 7557.
SABIO-RK; G0L322; -.
Proteomes; UP000008898; Chromosome.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0033916; F:beta-agarase activity; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
GO; GO:0008152; P:metabolic process; IDA:UniProtKB.
CDD; cd02178; GH16_beta_agarase; 1.
InterPro; IPR016287; Beta_agarase.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR000757; GH16.
InterPro; IPR026444; Secre_tail.
Pfam; PF00722; Glyco_hydro_16; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF49899; SSF49899; 1.
TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 539 Beta-agarase A.
/FTId=PRO_5000055268.
CHAIN 20 295 Beta-agarase A catalytic chain.
/FTId=PRO_5000055269.
DOMAIN 21 289 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
REGION 82 92 Substrate binding.
{ECO:0000269|PubMed:15062085}.
REGION 96 98 Substrate binding.
{ECO:0000269|PubMed:15062085}.
ACT_SITE 147 147 Nucleophile.
{ECO:0000305|PubMed:12970344}.
ACT_SITE 152 152 Proton donor.
{ECO:0000305|PubMed:12970344}.
BINDING 73 73 Substrate. {ECO:0000269|PubMed:15062085}.
BINDING 144 144 Substrate. {ECO:0000269|PubMed:15062085}.
BINDING 176 176 Substrate. {ECO:0000269|PubMed:15062085}.
BINDING 271 271 Substrate. {ECO:0000269|PubMed:15062085}.
MUTAGEN 147 147 E->S: Abolishes beta-agarase activity.
{ECO:0000269|PubMed:15062085}.
CONFLICT 84 84 P -> A (in Ref. 1; AAF21820).
{ECO:0000305}.
TURN 22 25 {ECO:0000244|PDB:1O4Y}.
STRAND 36 40 {ECO:0000244|PDB:1O4Y}.
HELIX 42 44 {ECO:0000244|PDB:1O4Y}.
STRAND 50 53 {ECO:0000244|PDB:1O4Y}.
HELIX 59 62 {ECO:0000244|PDB:1O4Y}.
STRAND 65 68 {ECO:0000244|PDB:1O4Y}.
STRAND 70 72 {ECO:0000244|PDB:1O4Y}.
STRAND 79 81 {ECO:0000244|PDB:1O4Y}.
HELIX 83 85 {ECO:0000244|PDB:1O4Y}.
STRAND 86 91 {ECO:0000244|PDB:1O4Y}.
STRAND 93 101 {ECO:0000244|PDB:1O4Y}.
STRAND 104 107 {ECO:0000244|PDB:1O4Y}.
STRAND 109 114 {ECO:0000244|PDB:1O4Y}.
STRAND 118 127 {ECO:0000244|PDB:1O4Y}.
STRAND 130 140 {ECO:0000244|PDB:1O4Y}.
STRAND 146 154 {ECO:0000244|PDB:1O4Y}.
HELIX 157 159 {ECO:0000244|PDB:1O4Y}.
HELIX 161 164 {ECO:0000244|PDB:1O4Y}.
STRAND 166 175 {ECO:0000244|PDB:1O4Y}.
TURN 176 179 {ECO:0000244|PDB:1O4Y}.
STRAND 180 182 {ECO:0000244|PDB:1O4Y}.
HELIX 187 189 {ECO:0000244|PDB:1O4Y}.
STRAND 190 192 {ECO:0000244|PDB:1O4Y}.
HELIX 198 200 {ECO:0000244|PDB:1O4Y}.
STRAND 203 211 {ECO:0000244|PDB:1O4Y}.
STRAND 214 219 {ECO:0000244|PDB:1O4Y}.
STRAND 222 227 {ECO:0000244|PDB:1O4Y}.
HELIX 229 232 {ECO:0000244|PDB:1O4Y}.
TURN 237 240 {ECO:0000244|PDB:1O4Y}.
STRAND 247 254 {ECO:0000244|PDB:1O4Y}.
TURN 257 259 {ECO:0000244|PDB:1O4Y}.
HELIX 265 269 {ECO:0000244|PDB:1O4Y}.
TURN 271 273 {ECO:0000244|PDB:1O4Y}.
STRAND 274 288 {ECO:0000244|PDB:1O4Y}.
SEQUENCE 539 AA; 60020 MW; 8D60A87DBF009A44 CRC64;
MKKNYLLLYF IFLLCGSIAA QDWNGIPVPA NPGNGMTWQL QDNVSDSFNY TSSEGNRPTA
FTSKWKPSYI NGWTGPGSTI FNAPQAWTNG SQLAIQAQPA GNGKSYNGII TSKNKIQYPV
YMEIKAKIMD QVLANAFWTL TDDETQEIDI MEGYGSDRGG TWFAQRMHLS HHTFIRNPFT
DYQPMGDATW YYNGGTPWRS AYHRYGCYWK DPFTLEYYID GVKVRTVTRA EIDPNNHLGG
TGLNQATNII IDCENQTDWR PAATQEELAD DSKNIFWVDW IRVYKPVAVS GGGNNGNDGA
TEFQYDLGTD TSAVWPGYTR VSNTTRAGNF GWANTNDIGS RDRGASNGRN NINRDINFSS
QTRFFTQDLS NGTYNVLITF GDTYARKNMN VAAEGQNKLT NINTNAGQYV SRSFDVNVND
GKLDLRFSVG NGGDVWSITR IWIRKVTSNS ANLLAAKGLT LEDPVETTEF LYPNPAKTDD
FVTVPNSEIG SSIIIYNSAG QVVKKVSVVS ENQKISLEGF AKGMYFINLN GQSTKLIVQ


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