ID   AGAR_PSEAF              Reviewed;         505 AA.
AC   P13734;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Beta-agarase;
DE            EC=3.2.1.81;
DE   Flags: Precursor;
GN   Name=agrA;
OS   Pseudoalteromonas atlantica (Alteromonas atlantica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2914859; DOI=10.1128/jb.171.1.602-605.1989;
RA   Belas R.;
RT   "Sequence analysis of the agrA gene encoding beta-agarase from Pseudomonas
RT   atlantica.";
RL   J. Bacteriol. 171:602-605(1989).
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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 86 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/AGAR/";
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DR   EMBL; M22725; AAA25696.1; -; Genomic_DNA.
DR   PIR; A32261; A32261.
DR   AlphaFoldDB; P13734; -.
DR   SMR; P13734; -.
DR   CAZy; GH86; Glycoside Hydrolase Family 86.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR040527; Porphyrn_cat_1.
DR   Pfam; PF18206; Porphyrn_cat_1; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..505
FT                   /note="Beta-agarase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012252"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   505 AA;  57617 MW;  66B75CBF486280B1 CRC64;
     MLKVIPWLLV TSSLVAIPTY IHATTEVVVN LNVKHSVEGK SEFERKNHIK LHSTLNDNDW
     QGEEDKLKYM MEELDVYFGR DNGGTVWNFN QAIEDPANIG YADPQNIIAR GQAQRETNWG
     QNKSALHQYD GRGDLMIGGQ PRAHYLGNTS PCCGGSAWQA KGGDAVGDFL GQYVNEFFRS
     AGDPVTKGHL APVYFEVLNE PLYQVTDAPH ELGLEQPIPP IDIFTFHNDV ADAFRQHNTH
     IKIGGFTVAF PIFEQREFAR WEERMKLFID TSGSHMDVYS THFYDLEDDN RFKGSRLEAT
     LDMIDQYSLL ALGETKPHVI SEYGGRNRPM ENAPWSALRD WWFLKTASPM LMQFLSRPDS
     VLTSIPFVPI KALWGTAADG TPYNWRLLRQ QKEAPNETGE NWVFTEMVKF YQLWSDVKGT
     RVDTFSTNSD FLIDSYVQND KAYVLISNLT EQAEKIVVHK YGAPASSQPT TRIKHLYLKG
     AAPRLMKQVM RQISKKSRLL LKRLW