ID A0A2M9HN61_9BIFI Unreviewed; 1475 AA.
AC A0A2M9HN61;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303};
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=CUU80_10470 {ECO:0000313|EMBL:PJM78250.1};
OS Bifidobacterium scaligerum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM78250.1, ECO:0000313|Proteomes:UP000228755};
RN [1] {ECO:0000313|EMBL:PJM78250.1, ECO:0000313|Proteomes:UP000228755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (NOV-2017) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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:PJM78250.1}.
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DR EMBL; PGLQ01000013; PJM78250.1; -; Genomic_DNA.
DR OrthoDB; 9763188at2; -.
DR Proteomes; UP000228755; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd10315; CBM41_pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.4270; Listeria-Bacteroides repeat domain; 6.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013378; InlB-like_B-rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR NCBIfam; TIGR02543; List_Bact_rpt; 2.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF09479; Flg_new; 6.
DR Pfam; PF03714; PUD; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000228755}.
FT DOMAIN 91..472
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 482..566
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 160313 MW; B959A37AABC55B8E CRC64;
MTRNTALRGL TASRSAEKPA HLNRRARTTM SRSLRKGASK LFAVMLGAAM TFGGAVATTA
AVADEIDANI TQQAASKKAG KTIDPTKAQS DVTMIAFQQS WNTIAKECKS TYGPEGVGYV
QISPPEESVQ GTQWWTVYQP ISYSLNSRFG TEDELKNMIT ECNSVGVQII ADVVLNHTSG
HDVSWVDDQY GVAGTAYNGT YGRYPGIGIY QYEESGNNHQ YGLASGDFHS CRTNIADYTN
ADEVQDCRLS TMWDINTGSS RVQNIQAEYL AKLWNLGVRG FRIDSAKHID TLDLKAIKAK
LAQKIGMKAA DIPFQQEVIY HQGESELLAP KHYTANGDVT EFSYSYQLRQ YFNGDISNLK
NISSGLLPSD KATVFVTNWD TARGSETLTV DSGSRYELAN AFMLAYDYGK PKLISDYYFT
DGNSDAGPNG TTDTHVTDVD FDEACKTSGT REQGQWLCEQ RWASVRGMIG FHNAVAGTTT
VGNWQHNGAN NIGFARQDAN GKDQGFIAIN NTLQEHQETY QTNLPNGEYC DVYTSGKTCN
KVTVKDGKLS VTIAKRSAVA IYAAADKPDN WVGYETADTG YDDQANTDRI GDGSATIYYK
PSTDWGNDVY IQYAIGDTLL NGKPVKMEKV SGDGADCDAA AGWYKTTIPD ATAKRLKYRF
TNDPNGSDGA LWDYHDGYSD EGGSKLYENA VGTAITAVEN HDETIGVPFV CVASAKTTFT
VHFKASTDAQ KKATGVVVWG TDVNGNALGK TYHAFDKTSD SYGKRMTTTL GGDFTTVNYR
IVAAEDGSVD ADAVAGTNDS YAASVIDKQE GSVVAKVRGS IEAWADGSDG KSYDSSEESR
NPASVPTPND VKNPKQLNVI VHYMRADGNY QEYDLDTDAW KGWDLWMWSG EQSGSPVSFT
EHDDYGMIAR YTLNQPTKGN RTPEFVLRQG GDSWMSKDPD GNDRLIPESA IQVAAGQNET
GTAEIWLVSG DPTIYTYRPS VLGVMFETGF DWNVSPQAVV YGGTVRPIAD SQVPKREGYI
LTGWTTDADG NDPFTIGEGG TPVTERLKLY AQYEKANVVT FDAGSDAGFD WRIDSQTVRT
GGTVSAPASN QNPDGHRDGY KLLGWSTTKG NKVADFQFDD GNGGGTQITG DTTLYAVWQK
LTYTVTFETG EGGSDVAPQT VEYGDAVSVP TSAPTRTGYD FVSWVTDVAE DGTPGNTPYV
FGTPVTGNLT LYAKWTQKGT TVHLVTLHHN DGTDAVDTNY VENGTSMTSP KMTRDGYRLA
GWSTKADGLD DLYDFSSQPV TGDLTLYAQW VKVWKVAFDL NYEDAPATGE DGSVPTQTVD
DGADAYATEP SPAPKREGYT FDGWYTDADL TTKFVFKGDA GDQPTLVTAD ITLYAKWVKE
GTKRTITFQP NGGSLGEGMP STQQVPDGEY LTKPKKNPTR TGYTFQGWTT VKNDAFASNK
NGTFSGGSAF GFDAYGKSLI PIDRDGTLYA LWSKD
//
