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Database: UniProt
Entry: G8RZK7_ACTS5
LinkDB: G8RZK7_ACTS5
Original site: G8RZK7_ACTS5 
ID   G8RZK7_ACTS5            Unreviewed;      1092 AA.
AC   G8RZK7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN   OrderedLocusNames=ACPL_3725 {ECO:0000313|EMBL:AEV84620.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV84620.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP003170; AEV84620.1; -; Genomic_DNA.
DR   RefSeq; WP_014690692.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8RZK7; -.
DR   STRING; 134676.ACPL_3725; -.
DR   KEGG; ase:ACPL_3725; -.
DR   PATRIC; fig|134676.3.peg.3639; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_284365_0_0_11; -.
DR   OMA; SRYYEYT; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000005440; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR018905; A-galactase_NEW3.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF10633; NPCBM_assoc; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:AEV84620.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:AEV84620.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1092
FT                   /note="1,4-alpha-D-glucan glucanohydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003515316"
FT   DOMAIN          872..982
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   1092 AA;  116404 MW;  723FC401FA560419 CRC64;
     MLKPARVSVL LTVLLALVAT PGTALAAPRP PRVHGQSVQA GHLRVQVLSP TLLRLEYAAD
     DHFEDQATFN AVDRAPGRTW FRAGTAHGEL RVWTGAVTLH YRLDSGPVTA ANTTLDLTVA
     GRRTSVHPGF GMQPADPLGG WYRGLDYYAG QAGPVDQLSL HPGLLDRQGW YLLDDTATAL
     RTGNGQLGAR PARTGAYQDG YLFGYGHDYP RALADLRTLT GPSVLPPEWA FGTWFSKYQA
     YSTADYRTTI LPAFKNHRVP LDSLVMDTDW KAPNQWAGWN WNPGLFPDPD AFLKQLRAAG
     VNATLNVHAA ISGDDPRFAQ AQATAKGRLQ PSTNSFAPNP YRFDWGDPDQ AAAFVQLHQP
     FEQQGVRQWW LDYCCDDSTV STPGVTPDSW VNELYRREGD ARGVRGFALS RIGAAFPAYT
     AIGPSGPWAE HRSTVHFTGD TEATFATLAF AAAMTPGEGA AIGQSYVSHD IGSFAGRHLS
     DDLYLRWVQL GAFQPILRLH SDHGDRLPWE YDSAVSGPAA DFLRLRESLV PYLYTAARQN
     YDTGLPMARA LYLNWPEQSE AYRHDSEYLL GDSLLVAPVT TPGLSTTAPV WFPPGTWTDL
     FTGETFRGPV TRTVGATPDH MPVYVRGGGI LAQRAGDVNV ATQPRDRLTL TAYPHGSGTA
     SVYEDNGDGL GYRTGRSARI PARYTEGRRA ALTVGPVQGT YPGAPTTRQY TVAFADVARP
     HRVTADGHSA AWTYDPGKHL LTVALPAIAA GRAVTVEHDG ATLTVAQKPA VDTTFTAPDG
     LQSGATSTLV ATATNHGPGA ITDVAATVTA PAGWVVTPKS ATTAARLAPG ATFTATYAAT
     PAGAAPRTQP VTVHIAYRNP DGTATSAPAA LTVPLKPVAV TFRVLAPPGT PPDATLYVPG
     SIAQLGPWDP GKQAMTDRGG GVWEATVSIL DGTDLQYKYT RGTWDRVEEW GSITGTDNRS
     VSVDGGLSHT MLVDDTSTAW GDASVPDSHK AIRYWRDPLV VTTEATARAV TVRFERDIRP
     TGADYSGSVT VAGPSGTVAG SVAEPSPGTL VFTPGAALPA GTYTGTVTGV TSAVSDGVPI
     QKPYTFTFAI AP
//
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