AGAC_ZOBGA
ID AGAC_ZOBGA Reviewed; 328 AA.
AC D7GXG5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Beta-agarase C;
DE EC=3.2.1.81;
DE Flags: Precursor;
GN Name=agaC; OrderedLocusNames=zobellia_4267;
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].
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 PROTEIN SEQUENCE OF 68-77, AND SUBCELLULAR 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 [4]
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).
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 (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}.
CC -!- INDUCTION: When cells are grown with the low sulfated agar.
CC {ECO:0000269|PubMed:22778272}.
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; FQ073843; CBM41187.1; -; Genomic_DNA.
DR EMBL; FP476056; CAZ98402.1; -; Genomic_DNA.
DR PDB; 6HY3; X-ray; 1.30 A; A=69-328.
DR PDBsum; 6HY3; -.
DR AlphaFoldDB; D7GXG5; -.
DR SMR; D7GXG5; -.
DR STRING; 63186.ZOBELLIA_4267; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAZ98402; CAZ98402; ZOBELLIA_4267.
DR KEGG; zga:ZOBELLIA_4267; -.
DR PATRIC; fig|63186.3.peg.4177; -.
DR HOGENOM; CLU_053494_0_0_10; -.
DR OMA; WNEEYHT; -.
DR OrthoDB; 1046649at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; SSF49899; 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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..67
FT /evidence="ECO:0000269|PubMed:15456406"
FT /id="PRO_0000422026"
FT CHAIN 68..328
FT /note="Beta-agarase C"
FT /id="PRO_0000422027"
FT DOMAIN 70..328
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 26..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 119..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D7GXG0"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:G0L322"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6HY3"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6HY3"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 204..208
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6HY3"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:6HY3"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:6HY3"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:6HY3"
FT STRAND 313..327
FT /evidence="ECO:0007829|PDB:6HY3"
SQ SEQUENCE 328 AA; 37612 MW; 932014A203B2FD37 CRC64;
MNLTKMAVFA ASLFCLACKN DIDTELEKKS IPESEIQKSE EKLPNEEELT PTDPDEETNK
EETVTANATY DFTGNTPPPA PQGMKWVKIS QLSDEFNNGF NTDKWTKSLW NYGVPVQMKA
ENSGVSDGKL WIKATLGNDP ERWFETSRVM SKAQVNYPMY TVSRIKGAHI SAYNTFWLNN
GNISNRNEID VIENNSNPSC NCQPDFPWQM NSQYFHVVND DTKRNKGNFD NRELSDANPL
KGVAWNEEYH TFGVWWKDAT HIQFYLDGEP AGSVVSARDF TRELNIIWDL WTVDADWLGG
LAKKEHLSNN NINTMKIDWI HTYQLVEE
