ID A0A662ZL03_9GAMM Unreviewed; 834 AA.
AC A0A662ZL03;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=SAMN02910344_02076 {ECO:0000313|EMBL:SFP69297.1};
OS Ruminobacter amylophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Ruminobacter.
OX NCBI_TaxID=867 {ECO:0000313|EMBL:SFP69297.1, ECO:0000313|Proteomes:UP000243745};
RN [1] {ECO:0000313|EMBL:SFP69297.1, ECO:0000313|Proteomes:UP000243745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1361 {ECO:0000313|EMBL:SFP69297.1,
RC ECO:0000313|Proteomes:UP000243745};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FOXF01000057; SFP69297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A662ZL03; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000243745; Unassembled WGS sequence.
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; cd00146; PKD; 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 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 InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_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 Pfam; PF00801; PKD; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..834
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025032993"
FT DOMAIN 642..724
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 834 AA; 92753 MW; 3207E666A965AC3A CRC64;
MHHNRINQIS RAVLTACLPV VSMAIFNVAG AQNYEEEMVI LHPFQWSYNS IAKECTEYLG
PAGFDGVQIS QPAEHISKKG VWWAVYQPVN FKNFTTMTGN ENELRAMIRT CNDAGVKVFA
DAVFNQRAGG SGTGLGGSSY QKRTRYADGF TSDDFHPGCR LYDYSSADNV RLCDLNGMPD
IKTESSSTQE KIADYLATLM NMGVHGFRID AAKHMKYTDI DSIIRKTAKK TGRRPPIYME
VIEGINEAAD IYPDKYTYIE NSVVTDFSYV QNIKNVFDSR KFGDALKLKA KYRGNSEVFV
NNHDDEYKRC SAGSCSMSTQ NNPYYHLAQS WMAVWPEGTV RQIYSGYSFS SHDPAGPVSA
SRCTGGWLCQ HREPIVLNAP RFARATRGKK VTTKGYDSGI LWFNRGSKGF YAMNPSGSDV
KHTFTVEMPD GDYCDILGAK DPARDPCGKE VKVRNGRVTL TIPAKSAMAI CTDENWCGRH
RDPCETDPYG AACLCKDQTV DKNGVCESFC SANPSDEKCF CLLNPDNEEC VNPIEKTKGL
LCYTGTSNSW KFEEMAYSKK TGLWTTEVTL SEDSGQSFKI VDGCDWSAGV IYGKSSTSGK
LKVNDSKEGN VPIDLRQGVY ELSIRDADMT YEFKDVTPVP EPPVPLAADF TCTVSGSTVE
FHNKTAFNPE DDIAYLWNFG NGETSSVEEP VVVYDSLGKH LVSLLASSRI SEESSRVTRY
VEITELTGNP KGETLCYSGT DTDWKMEPMI YNSTVGYWMR KVELDGSGSQ RFRIISGCSW
NEGNVLGGNG TSGVLIKSDS FAHDAVHDPE LKGTYRLLVK DNALEYRYNR YPDR
//
