ID   AGAA_VIBS7              Reviewed;         995 AA.
AC   P48839;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Beta-agarase A;
DE            EC=3.2.1.81;
DE   AltName: Full=Agarase 0107;
DE   Flags: Precursor;
GN   Name=agaA;
OS   Vibrio sp. (strain JT0107).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=47913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8285681; DOI=10.1128/aem.59.11.3750-3756.1993;
RA   Sugano Y., Matsumoto T., Kodama H., Noma M.;
RT   "Cloning and sequencing of agaA, a unique agarase 0107 gene from a marine
RT   bacterium, Vibrio sp. strain JT0107.";
RL   Appl. Environ. Microbiol. 59:3750-3756(1993).
CC   -!- FUNCTION: Hydrolyzes agarose and also neoagarotetraose to yield
CC       neoagarobiose.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 50 family. {ECO:0000305}.
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DR   EMBL; D14721; BAA03541.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48839; -.
DR   SMR; P48839; -.
DR   CAZy; GH50; Glycoside Hydrolase Family 50.
DR   BioCyc; MetaCyc:MON-16649; -.
DR   GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR040669; Agarase_CBM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF17992; Agarase_CBM; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..995
FT                   /note="Beta-agarase A"
FT                   /id="PRO_0000012215"
FT   REGION          936..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..965
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   995 AA;  107276 MW;  437142F6C254124B CRC64;
     MKIKFLSAAI AASLALPLSA ATLVTSFEEA DYSSSENNAE FLEVSGDATS EVSTEQATDG
     NQSIKASFDA AFKPMVVWNW ASWNWGAEDV MSVDVVNPND TDVTFAIKLI DSDILPDWVD
     ESQTSLDYFT VSANTTQTFS FNLNGGNEFQ THGENFSKDK VIGVQFMLSE NDPQVLYFDN
     IMVDGETVTP PPSDGAVNTQ TAPVATLAQI EDFETIPDYL RPDGGVNVST TTEIVTKGAA
     AMAAEFTAGW NGLVFAGTWN WAELGEHTAV AVDVSNNSDS NIWLYSRIED VNSQGETATR
     GVLVKAGESK TIYTSLNDNP SLLTQDERVS ALGLRDIPAD PMSAQNGWGD FVALDKSQIT
     AIRYFIGELA SGETSQTLVF DNMRVIKDLN HESAYAEMTD AMGQNNLVTY AGKVASKEEL
     AKLSDPEMAA LGELTNRNMY GGNPDSSPAT DCVLATPASF NACKDADGNW QLVDPAGNAF
     FSTGVDNIRL QDTYTMTGVS SDAESESALR QSMFTEIPSD YVNENYGPVH SGPVSQGQAV
     SFYANNLITR HASEDVWRDI TVKRMKDWGF NTLGNWTDPA LYANGDVPYV ANGWSTSGAD
     RLPVKQIGSG YWGPLPDPWD ANFATNAATM AAEIKAQVEG NEEYLVGIFV DNEMSWGNVT
     DVEGSRYAQT LAVFNTDGTD ATTSPAKNSF IWFLENQRYT GGIADLNAAW GTDYASWDAT
     SPAQELAYVA GMEADMQFLA WQFAFQYFNT VNTALKAELP NHLYLGSRFA DWGRTPDVVS
     AAAAVVDVMS YNIYKDSIAA ADWDADALSQ IEAIDKPVII GEFHFGALDS GSFAEGVVNA
     TSQQDRADKM VSFYESVNAH KNFVGAHWFQ YIDSPLTGRA WDGENYNVGF VSNTDTPYTL
     MTDAAREFNC GMYGTDCSSL SNATEAASRA GELYTGTNIG VSHSGPEAPD PGEPVDPPID
     PPTPPTGGVT GGGGSAGWLS LLGLAGVFLL RRRKV