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Beta-agarase C (EC 3.2.1.81)

 AGAC_ZOBGA              Reviewed;         328 AA.
D7GXG5;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 1.
25-OCT-2017, entry version 36.
RecName: Full=Beta-agarase C;
EC=3.2.1.81;
Flags: Precursor;
Name=agaC; OrderedLocusNames=zobellia_4267;
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].
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]
PROTEIN SEQUENCE OF 68-77, 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).
[4]
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).
-!- 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 (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-galactosidic
linkages in agarose, giving the tetramer as the predominant
product.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}.
-!- INDUCTION: When cells are grown with the low sulfated agar.
{ECO:0000269|PubMed:22778272}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
{ECO:0000305}.
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EMBL; FQ073843; CBM41187.1; -; Genomic_DNA.
EMBL; FP476056; CAZ98402.1; -; Genomic_DNA.
RefSeq; WP_013995590.1; NZ_MWRZ01000002.1.
CAZy; GH16; Glycoside Hydrolase Family 16.
EnsemblBacteria; CAZ98402; CAZ98402; ZOBELLIA_4267.
KEGG; zga:ZOBELLIA_4267; -.
PATRIC; fig|63186.3.peg.4177; -.
OMA; WNEEYHT; -.
Proteomes; UP000008898; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
InterPro; IPR016287; Beta_agarase.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000757; GH16.
Pfam; PF00722; Glyco_hydro_16; 1.
PIRSF; PIRSF001097; Agarase; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase;
Reference proteome; Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 67 {ECO:0000269|PubMed:15456406}.
/FTId=PRO_0000422026.
CHAIN 68 328 Beta-agarase C.
/FTId=PRO_0000422027.
DOMAIN 70 328 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
REGION 119 129 Substrate binding.
{ECO:0000250|UniProtKB:G0L322}.
REGION 133 135 Substrate binding.
{ECO:0000250|UniProtKB:G0L322}.
ACT_SITE 188 188 Nucleophile.
{ECO:0000250|UniProtKB:G0L322}.
ACT_SITE 193 193 Proton donor.
{ECO:0000250|UniProtKB:G0L322}.
BINDING 110 110 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 188 188 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 193 193 Substrate.
{ECO:0000250|UniProtKB:D7GXG0}.
BINDING 224 224 Substrate.
{ECO:0000250|UniProtKB:G0L322}.
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


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