ID I0YIP7_COCSC Unreviewed; 473 AA.
AC I0YIP7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
GN ORFNames=COCSUDRAFT_20858 {ECO:0000313|EMBL:EIE18266.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE18266.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE18266.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE18266.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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|ARBA:ARBA00000546,
CC ECO:0000256|RuleBase:RU000509};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIE18266.1}.
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DR EMBL; AGSI01000025; EIE18266.1; -; Genomic_DNA.
DR RefSeq; XP_005642810.1; XM_005642753.1.
DR AlphaFoldDB; I0YIP7; -.
DR STRING; 574566.I0YIP7; -.
DR GeneID; 17036173; -.
DR KEGG; csl:COCSUDRAFT_20858; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
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; IPR018238; Glyco_hydro_14_CS.
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.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 408..409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 473 AA; 52901 MW; 9E298AFC8B6E571E CRC64;
MPSTSLPVYV MLPLDTIWLL ERDGKSIPVI KREKALEVGL QTLRQAGVEG VMVDVWWGIV
ENAGPGKYDF SAYKRLFHKV AESGLKVQAV MSFHAAGGNV GDTCKISLPK WVQAVGAENP
DIYYTDRSGT RNRECLSLGC DSEPLFHGRT PVELYKGFIE AFADNFDYLF GDVITEITVG
LGPAGELRYP SYPEGDGRWR FPGVGEFQCF DRYMMASLRR AAEAVGHPEW GYDGPHDCGN
YNSAAWETGF FVSQGGSWDT EYGHFFLGWY SSLLLQHADR VLKAAAASLN KRGRPRKARA
AREHTDGHVV YEFDAACHLG VKLAGVHWWF KSRAHAAELT AGYYNTRERD GYAELMAMLR
RNNARLSFTC VEMRDCEHPP EGRCSPQGLL QQVIEAAAAA GVPLSGENAL QRYDHYAFDR
IAESAFGLNA RAGRLEQLTF LRMGDLMFDN WDAFSSFLHR LRSPPSTPNW TGY
//
