ID A0A7W7H573_9ACTN Unreviewed; 1080 AA.
AC A0A7W7H573;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN ORFNames=BJY16_007587 {ECO:0000313|EMBL:MBB4744128.1};
OS Actinoplanes octamycinicus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135948 {ECO:0000313|EMBL:MBB4744128.1, ECO:0000313|Proteomes:UP000546162};
RN [1] {ECO:0000313|EMBL:MBB4744128.1, ECO:0000313|Proteomes:UP000546162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45809 {ECO:0000313|EMBL:MBB4744128.1,
RC ECO:0000313|Proteomes:UP000546162};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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}.
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:MBB4744128.1}.
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DR EMBL; JACHNB010000001; MBB4744128.1; -; Genomic_DNA.
DR RefSeq; WP_239176967.1; NZ_BAABFG010000005.1.
DR AlphaFoldDB; A0A7W7H573; -.
DR Proteomes; UP000546162; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:TreeGrafter.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IEA:TreeGrafter.
DR CDD; cd06595; GH31_u1; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 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; CBM20.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR017853; GH.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF89; ALPHA-XYLOSIDASE; 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};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000546162};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1080
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5031339201"
FT DOMAIN 861..971
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 1080 AA; 116151 MW; 645D539245F7FCDD CRC64;
MVTRLAAWVA FLMLLVLTPG GALAAPRAPQ LHGQTVQAGH LRVQVLSPTL LRLEYSADDT
FEDRPTFNAV DRDPPRTRFT ASTRGGELRV TTSAVTLRHR LDSGPVTAAN TSLELRVGGR
PVTAHPEFGN PARADALGGW YRGLDYYAGQ AGPVEQLKLH PGMLNRGGWY LLDDTATALR
TDAGWVAARP ARTGAYQDGY LFGYGHDYRR GLADLRALTG PSALPPKWAF GTWFSKYQAY
SAEDYRTQLL PAFAENNVPL DSLVIDTDWK APNQWAGWNW NSTLFPKPEE FVDELSRKGI
TTTLNVHAAI SGDDPRFAGA QATAKGKLTP ATSSFAPNPY RFDWSDPDQA AAWTALHRPF
EDQGVRQWWL DYCCDDSRVT VPGLTADSWV NELYRRDGEA ADRRGFALSR IGASFPDYTT
PGPSGPWAEH RSTVHFTGDT RPDWATLAFA AAMTPAEASI GMSYVSHDIG SFAGKHLPDD
LYLRWVQLGA FQPILRLHSD HGDRLPWEYA GTVGKPAADF LRLREALVPY LYTAARQTYD
TGMPMARALY LQWPELDEAY QHDTQYLLGD SLLVAPVTTP GLSTTVPVWF PPGTWTDFFT
GETFRGPATR TVAATPDHMP VYVRAGGILP TAAPAPNVAA QPADRLTLTA YPHASGSTVV
YDDAGDGLGY RTGQYTRTPV RYDEGRRGAE LTVGPATRSR HYTVQFAGVS RPHLVTVAGR
RVPFTYDAAK HLISVEVTGA KAITVRHDGV PLTVAQQPAV ELTLTAPDGL QSGATSRLVL
AAHNAGPGTI TALTGSITAP DGWVVTPRTA TTAASLAPGA DFTVTYDVTP TGPSPRTAAV
TGHLAYRNPD GSAASLPASL TVPVRPVAVT FRVLAPPGTP PDATLHVPGN ITELGPWDPG
KVAMTNRGNG IHEATVTVLD GTDIQYKYTR GTWETVEDWG SITGTNNRSV TVDGGITRTM
LVDDTSTQWG VPGVPDTHLA IQYWRDPLVV NTATTPTAVT VTFQRDIQPT GADYSASITV
TGPTGPTAGA TTEPTPGALI WTPATPLPPG SYTLTVDQVS STGPGGVPIR KPYTSTFTVP
//
