ID   AGA34_AGAAL             Reviewed;          10 AA.
AC   P85974;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-MAY-2023, entry version 11.
DE   RecName: Full=Beta-agarase AgaA34 {ECO:0000303|PubMed:18071641};
DE            EC=3.2.1.81;
DE   Flags: Fragment;
OS   Agarivorans albus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Agarivorans.
OX   NCBI_TaxID=182262;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=YKW-34 {ECO:0000269|PubMed:18071641};
RX   PubMed=18071641; DOI=10.1007/s00253-007-1303-3;
RA   Fu X.T., Lin H., Kim S.M.;
RT   "Purification and characterization of a novel beta-agarase, AgaA34, from
RT   Agarivorans albus YKW-34.";
RL   Appl. Microbiol. Biotechnol. 78:265-273(2008).
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:18071641};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.117 uM for agarose {ECO:0000269|PubMed:18071641};
CC         KM=0.333 uM for neoagarotetraose {ECO:0000269|PubMed:18071641};
CC         Vmax=529 umol/min/mg enzyme toward agarose
CC         {ECO:0000269|PubMed:18071641};
CC         Vmax=313 umol/min/mg enzyme toward neoagarotetraose
CC         {ECO:0000269|PubMed:18071641};
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 6.0 to 10.0.
CC         {ECO:0000269|PubMed:18071641};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Active at temperatures up
CC         to 50 degrees Celsius. {ECO:0000269|PubMed:18071641};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18071641}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000269|PubMed:18071641}.
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DR   SABIO-RK; P85974; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0033916; F:beta-agarase activity; IDA:UniProtKB.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted.
FT   CHAIN           1..>10
FT                   /note="Beta-agarase AgaA34"
FT                   /id="PRO_0000347325"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:18071641"
SQ   SEQUENCE   10 AA;  1053 MW;  47541E19D5A1B2C7 CRC64;
     ASLVTSFEEA
//