AGAA_ZOBGA
ID AGAA_ZOBGA Reviewed; 539 AA.
AC G0L322; Q9RGX9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Beta-agarase A;
DE EC=3.2.1.81;
DE Contains:
DE RecName: Full=Beta-agarase A catalytic chain;
DE Short=AgaAc;
DE Flags: Precursor;
GN Name=agaA; OrderedLocusNames=zobellia_4203;
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], PROTEIN SEQUENCE OF 116-125, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RX PubMed=15456406; DOI=10.1042/bj20041044;
RA Jam M., Flament D., Allouch J., Potin P., Thion L., Kloareg B., Czjzek M.,
RA Helbert W., Michel G., Barbeyron T.;
RT "The endo-beta-agarases AgaA and AgaB from the marine bacterium Zobellia
RT galactanivorans: two paralogue enzymes with different molecular
RT organizations and catalytic behaviours.";
RL Biochem. J. 385:703-713(2005).
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 INDUCTION.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 20-295, AND ACTIVE SITE.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RX PubMed=12970344; DOI=10.1074/jbc.m308313200;
RA Allouch J., Jam M., Helbert W., Barbeyron T., Kloareg B., Henrissat B.,
RA Czjzek M.;
RT "The three-dimensional structures of two beta-agarases.";
RL J. Biol. Chem. 278:47171-47180(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 20-290 OF MUTANT SER-147 IN
RP COMPLEX WITH GALACTOSE, AND MUTAGENESIS OF GLU-147.
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RX PubMed=15062085; DOI=10.1016/j.str.2004.02.020;
RA Allouch J., Helbert W., Henrissat B., Czjzek M.;
RT "Parallel substrate binding sites in a beta-agarase suggest a novel mode of
RT action on double-helical agarose.";
RL Structure 12:623-632(2004).
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:15456406}.
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:15456406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for agarose {ECO:0000269|PubMed:15456406};
CC Note=kcat is 150 sec(-1).;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15062085,
CC ECO:0000269|PubMed:15456406}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}.
CC -!- INDUCTION: When cells are grown with the low sulfated agar.
CC {ECO:0000269|PubMed:22778272}.
CC -!- PTM: Proteolytically cleaved into mature beta-agarase A catalytic chain
CC (AgaAc). {ECO:0000269|PubMed:15456406}.
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; AF098954; AAF21820.1; -; Genomic_DNA.
DR EMBL; FP476056; CAZ98338.1; -; Genomic_DNA.
DR PDB; 1O4Y; X-ray; 1.48 A; A=20-295.
DR PDB; 1URX; X-ray; 1.70 A; A=20-290.
DR PDBsum; 1O4Y; -.
DR PDBsum; 1URX; -.
DR AlphaFoldDB; G0L322; -.
DR SMR; G0L322; -.
DR STRING; 63186.ZOBELLIA_4203; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAZ98338; CAZ98338; ZOBELLIA_4203.
DR KEGG; zga:ZOBELLIA_4203; -.
DR HOGENOM; CLU_037753_0_0_10; -.
DR BioCyc; MetaCyc:MON-16651; -.
DR BRENDA; 3.2.1.81; 7557.
DR SABIO-RK; G0L322; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0033916; F:beta-agarase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR CDD; cd02178; GH16_beta_agarase; 1.
DR InterPro; IPR016287; Beta_agarase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR026444; Secre_tail.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..539
FT /note="Beta-agarase A"
FT /id="PRO_5000055268"
FT CHAIN 20..295
FT /note="Beta-agarase A catalytic chain"
FT /id="PRO_5000055269"
FT DOMAIN 21..289
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12970344"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12970344"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT BINDING 82..92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15062085"
FT MUTAGEN 147
FT /note="E->S: Abolishes beta-agarase activity."
FT /evidence="ECO:0000269|PubMed:15062085"
FT CONFLICT 84
FT /note="P -> A (in Ref. 1; AAF21820)"
FT /evidence="ECO:0000305"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:1O4Y"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1O4Y"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1O4Y"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1O4Y"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:1O4Y"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1O4Y"
FT STRAND 274..288
FT /evidence="ECO:0007829|PDB:1O4Y"
SQ 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
