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Database: UniProt
Entry: A0A087SCW7_AUXPR
LinkDB: A0A087SCW7_AUXPR
Original site: A0A087SCW7_AUXPR 
ID   A0A087SCW7_AUXPR        Unreviewed;      2211 AA.
AC   A0A087SCW7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=F751_2830 {ECO:0000313|EMBL:KFM23571.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM23571.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM23571.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM23571.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
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}.
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DR   EMBL; KL662095; KFM23571.1; -; Genomic_DNA.
DR   RefSeq; XP_011396445.1; XM_011398143.1.
DR   GeneID; 23614221; -.
DR   KEGG; apro:F751_2830; -.
DR   eggNOG; KOG1064; Eukaryota.
DR   OrthoDB; 5480252at2759; -.
DR   Proteomes; UP000028924; 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; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR022033; Rav1p_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR31352:SF61; BETA-AMYLASE; 1.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 2.
DR   Pfam; PF12234; Rav1p_C; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 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:UP000028924}.
FT   DOMAIN          1395..1527
FT                   /note="RAVE complex protein Rav1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12234"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1369..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1802..1822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        473
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ   SEQUENCE   2211 AA;  228750 MW;  65EB182742E2F45F CRC64;
     MVPQAAWEAG QPGSHSNFQS ARVSMGEEEP ASCATTSVPV MVMLPLDTVN ADGVFRYASS
     KWFLPAIRQL AATGIHGVAV DVWWGAVERS PRRYDWSGYR QLFSAIKPLG LKFQVVMSFH
     ACGGNVGDNA LVPLPPWVHK VGDSDPDIFF TDRPRESSPG QRNREYISWF AETEPGLLRG
     RSVMECYIDF MRAFRDEFMG ELGSLIEEVV VGSGPCGELR YPAYPETNGW RFPGIGEFQC
     YDRRALASLA RAAGAAGHPE WGNSGPSNAG SYNSHPEETG FFQTWNGGWQ SPQGEFFLGW
     YSDALLEHGE RMLTAVTSVF NSPGGSSSGD PSPRSSDTMV GSPHTSVGVG GTPPPANGTP
     DGMMAAVSFA GMASPGGAGG FNGPFGSASL LPPAARPDQD HAAELTAGYY NTPERDGYAA
     LCALCARHGA AATLTCVEMC DAQHPPEALC GPEGVLRQVR EAAAAHGVPL AGENALPCFM
     PASVDEAALA RILPPLRGCT FLRLTRELMA PSYQEHWVRF MAQMKVNESA RPSGDSVPLH
     TLLVTPVAAS PSDPVVLVRW GGGPTALVAA ATASELVVVS LAGTLGIGPW ESHAGTRTGK
     VVARRPLPSP LSGCSWTARV DGLFVCLADG TLSMLRLDWP ARRLTEHWTI RPPEAQGTLA
     AGQSPAAPAA SAAAPACRDP AVSVWWPPAE SGAQGSGARR EKLRHPCPVL GLAWSRRLDS
     FFCMAMVIQG PAQGFYPGSL RAAWAEEEPE GPPGMEPAGT APHISTLTRV HVVRALQAVV
     VSSWRAEEGP SSAGPGAVTS AQAVLWGQLE QRRPRGAHHM DSPPSLTCRL EAREGSSTIL
     VRIDCSRFAT VPAAVQEPGT FFRPRPTPRT AGLPPALTLL SAWRGAATGH ATPVIDIAGS
     PYGGQLGSLD SGGPASDGDT RSRPLRRRWR TQDAALALAT TGDLVVVGGT GDALVEALPP
     GTRAVALHAI AVAGGDRGAA LLLLETAAQD RAGPRLAWTL RWGKERSLTG CAEGAWGGAE
     HVRVLGAGLD LLLSAERGAL RAWRAVERDG ESGAELVPAG LYALPDEATV LVAAAGACGL
     VAALTGGPAL ADSTPLADAS AGKKAADPPT LLLHVWRGRH AAVQTLPPLA RDGVTTAASL
     AWVPHAVAPA LAVVLGADAL LYCQQPGGRT IAARHGPLPA HGATTLAALL ACGAPGVAVH
     LLIARAAALE GGAPGGEAEA ALQRALAALW AAWSVALRLP ALLAGLREAT ATHVHGWERE
     RNDPDLPDPE RVTAAICRLG SNGGGALARV LAASDSAGHA RLDPAGRAFL DLARAAGHHG
     MPQGGLAASL QLHSGLGLEA VVWALMSGTQ EVLLEEALPS LAAAVDGSTA ASESGPSAAP
     SFLGTRADAG HAQPPTWEAL RAAGAGFWLR DPGLVLDVGE KLAKAQFAAA RKPDACALLY
     VALGKKATLQ GLYRTTNARK QADFLGRDFG LPANAQSAAK NAFVLLGQHR FSLAAAFFLL
     GGHVSDALDV CVRELSDLQL ALFIRRIVVL VMGGKGGGVD HASGPNAPAA PHHLEDWGWG
     AAARAALLGD DAGLLCALCW RVRWERGGAL AAAQLPALAA ALLPHIVGVE AAVYDVKRER
     DGDAIDDADH ATLLAQQLRG ALTAAATSLD AARLPLLALG SAAAAIAIGP AAKEGEETGL
     SKTLDPLTPF LARLAASALE MAFAPEALPE RLGSERDSSC STLGLGALSR VSSSSRGGGE
     GTAAAAWELK RQPIVCVDGD RCGALALCSL TSPDELGGRA LVVSTHRHGL VASDVIPLES
     AAHRGAAEAG SRPETPVSTP DVGGFQAPAA QGGIFSRIIS HIFDQASWEE SEKWGSSTMA
     ESDLGFGGFV GGPTSPHTPP ARGHIDGLPE LGSMHASALC AHPTRQFFLS ADGHGFVHLW
     QFGEREALAS FTPLPPPDLA SWGSGSLLSM GSRLFSGSLT SQLGGWGCCQ DLAWSPAADA
     FAAVGEGGVV ATWRLGRPKG VDADGHACAE WWHQCLARKG RAVTYIDEAV LAVGGEDASG
     NLVLWDSRAC SAVARLHPTT PGDGVTRLLG PSSGLWSLAA GTVGGAVVAL DLRRLSGAAA
     QPAAVGAGAP PALLWQAAHK KAGAVTALTR LAGGWVAAGY ADGDLRMFDP GLPSAPLVLR
     EERAHGARSR RRAAVSGLAG CPEGLVSAGA DGAVFLWTLE RSPEGQSSDY N
//
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