ID A0A2K0X571_9BIFI Unreviewed; 552 AA.
AC A0A2K0X571;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=BFS08_01620 {ECO:0000313|EMBL:PNP89680.1};
OS Gardnerella sp. KA00735.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1973156 {ECO:0000313|EMBL:PNP89680.1, ECO:0000313|Proteomes:UP000236541};
RN [1] {ECO:0000313|Proteomes:UP000236541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00735 {ECO:0000313|Proteomes:UP000236541};
RA Bumgarner R.E., Fredricks D.N., Srinivasan S.;
RL Submitted (NOV-2016) 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 ECO:0000256|RuleBase:RU361134};
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:PNP89680.1}.
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DR EMBL; NBMV01000001; PNP89680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0X571; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000236541; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..416
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 425..504
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 552 AA; 61332 MW; 29975D1137C8D449 CRC64;
MIHNAKFCVK MCNVRKNKTN IKSYAIIAFI LSLALLALSI IPFNSAFASS ADNKSLAFSK
GVIVTAFQQN WNSVAKECEQ TYGPEGVKYV QVSPPQDHIK GEAWWTSYQP VSYSLNSKLG
TEAEFKNMIT TCKAKGVGII ADAVINHMTG FDNKDTVGVG GSKYDASTQT FTDAGYTKDD
FHQIAESISN YNDPEQVWNY RLVGLLDLDT SKAHVREVLG KYFAKLLNLG VAGFRVDAVK
HMSPEDVKGI KQAAALAAHT TPDKIWWMQE TIGDINGSKK VQPDQYLATG EVDEFEYSHR
LRNYFYGSIE NLKHITDNLI PSDKAAIFVT NWDTERDSST RVLTYKDDEK YELANAFMLA
YPYGTPNIYS GYKFAKRDEG APGATVTSVP NVTCGKDSNW QCTQRWTSIR GMIGFYNAVK
GTKVTKWQDD DDNNIAFSRE NKGFLAINNT DNPHKVSYKT DLPDGEYCNV YVSNKCAHTV
NVSDGKIDTT IPANSAVAIH VKAVKSFGNS SRRTMIIWVF AVIALVFAFL INRHIASRNI
KLKNSSASST SN
//
