AGB34_AGAAL
ID AGB34_AGAAL Reviewed; 453 AA.
AC A8W969;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Beta-agarase AgaB34 {ECO:0000250|UniProtKB:P85974, ECO:0000303|Ref.1};
DE EC=3.2.1.81;
DE Flags: Precursor;
GN Name=agaB34 {ECO:0000312|EMBL:ABW77762.1};
OS Agarivorans albus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=182262;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABW77762.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YKW-34 {ECO:0000312|EMBL:ABW77762.1};
RA Fu X.T., Lin H., Pan C.-H., Kim S.M.;
RT "Gene cloning, expression, and characterization of a beta-agarase, AgaB34,
RT from Agarivorans albus YKW-34.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250|UniProtKB:P85974}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000250|UniProtKB:P85974}.
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DR EMBL; EU200967; ABW77762.1; -; Genomic_DNA.
DR AlphaFoldDB; A8W969; -.
DR SMR; A8W969; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR BRENDA; 3.2.1.81; 9574.
DR BRENDA; 3.2.1.B1; 9574.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0033916; F:beta-agarase activity; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR CDD; cd02178; GH16_beta_agarase; 1.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR016287; Beta_agarase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycosidase; Hydrolase; Lectin; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255, ECO:0000312|EMBL:ABW77762.1"
FT CHAIN 24..453
FT /note="Beta-agarase AgaB34"
FT /evidence="ECO:0000312|EMBL:ABW77762.1"
FT /id="PRO_0000347324"
FT DOMAIN 24..301
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT DOMAIN 313..453
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000312|EMBL:ABW77762.1"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07883"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P07883"
FT DISULFID 327..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000312|EMBL:ABW77762.1"
FT DISULFID 375..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000312|EMBL:ABW77762.1"
FT DISULFID 423..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000312|EMBL:ABW77762.1"
SQ SEQUENCE 453 AA; 50998 MW; 51C5FA72C4FB1BEF CRC64;
MKGFTKHSIL MACSIGLAIN ATAADWDNIP IPAELDAGQS WELQQNYSDS FNYSGKNSTF
TGKWKDSYFH SWTGPGLTHW SSDESWVGDG NLIISASRRQ GTNKVNAGVI TSKTKVKYPI
FLEASIKVSN LELSSNFWLL SENDQREIDV LEVYGGARQD WYAKNMSTNF HVFFRNNDNS
IKNDYNDQTH FTPTWGNYWR DGFHRFGVYW KSPTDVTFYI DGQKTTKGAW SQVVMKDKDY
TGAILDKSRY NMDQEAFIII DTEDHSWRSE AGHIATDADL ADSDKNKMYV DWIRVYKPTG
GSTTPPTGDI TPPSGYTNLQ LAHSNRCVDV INGALWNGST YQQYSCNTGN NNQRFKFTKI
ANNQYSINAK VSQLCMELAS GSSANGAKVQ QWICNHANSN QTWSLEDKGS NTFEIRNKQS
GKCLEVANSS NANGGQIRQW ACTGATNQRF KFL
