ID   AAGAR_ALTAG             Reviewed;        1429 AA.
AC   Q9LAP7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Alpha-agarase {ECO:0000312|EMBL:AAF26838.1};
DE            EC=3.2.1.158;
DE   Flags: Precursor;
GN   Name=agaA {ECO:0000312|EMBL:AAF26838.1};
OS   Alteromonas agarilytica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=105692;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF26838.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-43 AND
RP   802-821.
RC   STRAIN=GJ1B {ECO:0000312|EMBL:AAF26838.1};
RX   PubMed=17513582; DOI=10.1128/aem.00496-07;
RA   Flament D., Barbeyron T., Jam M., Potin P., Czjzek M., Kloareg B.,
RA   Michel G.;
RT   "Alpha-agarases define a new family of glycoside hydrolases, distinct from
RT   beta-agarase families.";
RL   Appl. Environ. Microbiol. 73:4691-4694(2007).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RX   PubMed=8513809; DOI=10.1111/j.1432-1033.1993.tb17959.x;
RA   Potin P., Richard C., Rochas C., Kloareg B.;
RT   "Purification and characterization of the alpha-agarase from Alteromonas
RT   agarlyticus (Cataldi) comb. nov., strain GJ1B.";
RL   Eur. J. Biochem. 214:599-607(1993).
CC   -!- FUNCTION: Alpha-agarase. Does not hydrolyze agarotetraose,
CC       agarohexaose, kappa-carrageenan, iota-carrageenan or lambda-
CC       carrageenan. {ECO:0000269|PubMed:8513809}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of 1,3-alpha-L-galactosidic linkages in
CC         agarose, yielding agarotetraose as the major product.; EC=3.2.1.158;
CC         Evidence={ECO:0000269|PubMed:8513809};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:8513809};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2. Active between pH 6.0 and 9.0.
CC         {ECO:0000269|PubMed:8513809};
CC       Temperature dependence:
CC         Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:8513809};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8513809}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 96 family. {ECO:0000255}.
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DR   EMBL; AF121273; AAF26838.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LAP7; -.
DR   CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR   CAZy; GH96; Glycoside Hydrolase Family 96.
DR   KEGG; ag:AAF26838; -.
DR   BioCyc; MetaCyc:MON-16655; -.
DR   BRENDA; 3.2.1.158; 8321.
DR   GO; GO:0033953; F:alpha-agarase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.1080.10; -; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   Pfam; PF03422; CBM_6; 3.
DR   Pfam; PF02412; TSP_3; 5.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF103647; SSF103647; 3.
DR   SUPFAM; SSF49785; SSF49785; 3.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS51175; CBM6; 3.
DR   PROSITE; PS51820; PA14; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Metal-binding; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:17513582"
FT   CHAIN           27..1429
FT                   /note="Alpha-agarase"
FT                   /evidence="ECO:0000269|PubMed:17513582"
FT                   /id="PRO_5000055969"
FT   DOMAIN          29..161
FT                   /note="CBM6 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          211..345
FT                   /note="CBM6 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          490..638
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   DOMAIN          662..793
FT                   /note="CBM6 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   REGION          349..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        42..43
FT                   /note="TY -> FF (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1429 AA;  154671 MW;  2ADD331171CBB5DC CRC64;
     MFKTKRSLLN SSIAISFAVL GVQAQAETLE LQAESFANSG GTYSDGQPNP VTIYNVNGQG
     AINFVNAGDY VDYNINALGG EYDIEYFVGT GVTSGPNIEV LVDVNGTWQS QGSVAVPYGS
     WDDFQSLTPS HTVTLPVGTS TVRLLAVGST WQWNLESFRL TQVSPVEPVG DADNDGVNDN
     QDLCPNSPSG VTVDNNGCQI TGGTDPGGES FVIQMEAFDS TGSDDSRAKG VIIGERGYPQ
     DKHTVVDSVQ TTDWVDYSIN FPSSANYSVS MLASGQTDHA TAVLYLDGTE INEVPVHTGS
     QADFANFQLA GSVYIASGTH TIRVQAQSST GEFSWLWFGD ALTFTNLDSD GGNGGEATQD
     ADNDGVLDSS DSCPNTPTGE PADVTGCSAS QLDDDNDGVS NNVDQCPNTV AGTEVDADGC
     EVIFADADND GIEDSQDFCP NTPAGEAVNN SGCGASQLDA DNDGVTNNID QCPNTPAGTQ
     VDASGCETDN GGEPGDSYYH NGQGLLFGRV DGATNFLGEE GYVANPDNYD VTTDLLETDD
     AIRANSTEVF RGEIYDADGH IAFYEHIDDS VRLYIDGQLV LSNDSWENSS QTTDLNLTPG
     WHNFELRLGN ADGGSGAVSG IGFGIDVDGG TNFVHPSNLS PSMFRASGQV VVDPILPPSG
     GIYIQLEDFD ETGTVGRVAS DPNDGFVKGD SNVGWVTNGD WGKYHNVFLE AGTYRAFITV
     STPAGGSYGA RVDIDGEPFA WGYFDSTGGW DIAAEYELYG GHLVVESTGN HTLHVEAVGG
     SDWQWSGDLV RLAKVSDSAV KQPRVYNPNE HIVAEIQGPA TGLQYLKTPV EIPLANKVLK
     SDVWYTYPQN RNLVVDGDTP YADFGATGAF WGHPPEHDFY DDTVIMDWAV NVVDDFQSEG
     FEYTARGEFD WGYGWFTEFT TNPQPHYVQT LDGRNVRMTF MGYLSHDGYN NNWLSNHSPA
     FVPFMKSQVD QILKANPDKL MFDTQTNSTR STDMRTFGGD FSPYAMENFR VWLLKKYSNA
     QLVSMGINDI TSFDYGAYLR AQGITHTDWS NAGDTISGNI PMMEDFIYFN RDVWNQKFAE
     VLEYIRQQRP NIEIGASTHL FESRGYIFNE NITFLSGELN LGARTSISEL PTNILVHLKG
     AQAVDKTLAY FPYPWEFDEL RIQNAPRFGR GWVAQAYAYG GLFSIPANVW VGGEVFTWSP
     GADNYRDIYQ FVRAQANLLD GYTSYAKAGY VHAMFSSMKA GFIDGGNQVQ SSVKILTEDN
     INFDMLVFGD AGYPVVPRQA DFDKFEYIFY DGDLNYLTAE QQAVLDAQGS KVKHIGQRGT
     IAGLQINVSI NGSVSNETVS AVSRIHETDS TAPYVVHLIN RPFAGGVTPI LNNVEVAIPA
     SYFPQGVTSA KLHLPDGSSS TVAVSTNANG DTVVSVSNLE VWGILELAH