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Alpha-agarase (EC 3.2.1.158)

 AAGAR_ALTAG             Reviewed;        1429 AA.
Q9LAP7;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-MAY-2017, entry version 51.
RecName: Full=Alpha-agarase {ECO:0000312|EMBL:AAF26838.1};
EC=3.2.1.158;
Flags: Precursor;
Name=agaA {ECO:0000312|EMBL:AAF26838.1};
Alteromonas agarilytica.
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Alteromonas.
NCBI_TaxID=105692;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF26838.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-43 AND
802-821.
STRAIN=GJ1B {ECO:0000312|EMBL:AAF26838.1};
PubMed=17513582; DOI=10.1128/AEM.00496-07;
Flament D., Barbeyron T., Jam M., Potin P., Czjzek M., Kloareg B.,
Michel G.;
"Alpha-agarases define a new family of glycoside hydrolases, distinct
from beta-agarase families.";
Appl. Environ. Microbiol. 73:4691-4694(2007).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBUNIT.
PubMed=8513809; DOI=10.1111/j.1432-1033.1993.tb17959.x;
Potin P., Richard C., Rochas C., Kloareg B.;
"Purification and characterization of the alpha-agarase from
Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B.";
Eur. J. Biochem. 214:599-607(1993).
-!- FUNCTION: Alpha-agarase. Does not hydrolyze agarotetraose,
agarohexaose, kappa-carrageenan, iota-carrageenan or lambda-
carrageenan. {ECO:0000269|PubMed:8513809}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of 1,3-alpha-L-galactosidic
linkages in agarose, yielding agarotetraose as the major product.
{ECO:0000269|PubMed:8513809}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:8513809};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.2. Active between pH 6.0 and 9.0.
{ECO:0000269|PubMed:8513809};
Temperature dependence:
Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:8513809};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8513809}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 96 family.
{ECO:0000255}.
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EMBL; AF121273; AAF26838.1; -; Genomic_DNA.
ProteinModelPortal; Q9LAP7; -.
SMR; Q9LAP7; -.
CAZy; CBM6; Carbohydrate-Binding Module Family 6.
CAZy; GH96; Glycoside Hydrolase Family 96.
KEGG; ag:AAF26838; -.
KO; K20851; -.
BioCyc; MetaCyc:MONOMER-16655; -.
BRENDA; 3.2.1.158; 8321.
GO; GO:0033953; F:alpha-agarase activity; IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
Gene3D; 2.60.120.260; -; 3.
InterPro; IPR006584; Cellulose-bd_IV.
InterPro; IPR029070; Chitinase_insertion.
InterPro; IPR005084; CMB_fam6.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR003367; Thrombospondin_3-like_rpt.
InterPro; IPR028974; TSP_type-3_rpt.
Pfam; PF03422; CBM_6; 3.
Pfam; PF02412; TSP_3; 5.
SMART; SM00606; CBD_IV; 1.
SUPFAM; SSF103647; SSF103647; 3.
SUPFAM; SSF49785; SSF49785; 3.
SUPFAM; SSF54556; SSF54556; 1.
PROSITE; PS51175; CBM6; 3.
PROSITE; PS51820; PA14; 1.
1: Evidence at protein level;
Calcium; Carbohydrate metabolism; Direct protein sequencing;
Glycosidase; Hydrolase; Metal-binding; Polysaccharide degradation;
Repeat; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:17513582}.
CHAIN 27 1429 Alpha-agarase.
{ECO:0000269|PubMed:17513582}.
/FTId=PRO_5000055969.
DOMAIN 29 161 CBM6 1. {ECO:0000255|PROSITE-
ProRule:PRU00523}.
DOMAIN 211 345 CBM6 2. {ECO:0000255|PROSITE-
ProRule:PRU00523}.
DOMAIN 490 638 PA14. {ECO:0000255|PROSITE-
ProRule:PRU01164}.
DOMAIN 662 793 CBM6 3. {ECO:0000255|PROSITE-
ProRule:PRU00523}.
CONFLICT 42 43 TY -> FF (in Ref. 1; AA sequence).
{ECO:0000305}.
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


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