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Database: UniProt
Entry: A4RUJ6_OSTLU
LinkDB: A4RUJ6_OSTLU
Original site: A4RUJ6_OSTLU 
ID   A4RUJ6_OSTLU            Unreviewed;       480 AA.
AC   A4RUJ6;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN   ORFNames=OSTLU_14648 {ECO:0000313|EMBL:ABO95263.1};
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO95263.1, ECO:0000313|Proteomes:UP000001568};
RN   [1] {ECO:0000313|EMBL:ABO95263.1, ECO:0000313|Proteomes:UP000001568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901 {ECO:0000313|EMBL:ABO95263.1,
RC   ECO:0000313|Proteomes:UP000001568};
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive maltose units from the
CC         non-reducing ends of the chains.; EC=3.2.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU000509};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC       {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
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DR   EMBL; CP000583; ABO95263.1; -; Genomic_DNA.
DR   RefSeq; XP_001416970.1; XM_001416933.1.
DR   AlphaFoldDB; A4RUJ6; -.
DR   STRING; 436017.A4RUJ6; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   EnsemblPlants; ABO95263; ABO95263; OSTLU_14648.
DR   GeneID; 5000608; -.
DR   Gramene; ABO95263; ABO95263; OSTLU_14648.
DR   KEGG; olu:OSTLU_14648; -.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_5_1_1; -.
DR   OMA; CIEMKDV; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000001568; Chromosome 3.
DR   GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352:SF61; BETA-AMYLASE; 1.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {ECO:0000256|RuleBase:RU000509};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001568}.
FT   REGION          450..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        169
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         379..380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         422
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   480 AA;  54059 MW;  196F130E8336DEEC CRC64;
     MLPLNVVTND GEVNDPEALE RGLRALSEIG VEGVMIDVWW GIVERDGPRK YDWAAYREVI
     DMIKDAGLKV QAVMSFHACG ANVGDVVEIP LPDWVLEAGK KDPDLFFTDQ YGYRNPECIS
     LWADNAATLA GRTPMNTYKD FMISFRNTFK AELGTTLTEI AVGCGPCGEL RYPAYPENRF
     AQKASQWRFP GIGEFQCYDQ RSLLSLSRAA SEAGHIEWGG SGPHDTGGYN NLPFETGFFR
     YDGGSWDSEY GSFFLSWYSS ELVNHGDRML EMTKRVFDKR GVTLAIKCAG VHWWYNVRSH
     AAELTAGYFN TRAGEFVSER DGYAPIVRVC KKHGARLNFT CVEMHDSDHP WYCYCGPEGL
     LRQIRSACAR FDVPFAGENA LCRFDQAAYD KIIKNCAGEG NDEEMWREGT MLPPMACFTF
     LRFNAELFSP FAFESFRIFV QRMRDETGLL DTSIGNTSDE EASTEDVDEI SSESRVQLGL
//
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