ID A0A3S2WNC1_9BURK Unreviewed; 612 AA.
AC A0A3S2WNC1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=EOD73_13755 {ECO:0000313|EMBL:RVT83870.1};
OS Inhella crocodyli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Inhella.
OX NCBI_TaxID=2499851 {ECO:0000313|EMBL:RVT83870.1, ECO:0000313|Proteomes:UP000288587};
RN [1] {ECO:0000313|EMBL:RVT83870.1, ECO:0000313|Proteomes:UP000288587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-18 {ECO:0000313|EMBL:RVT83870.1,
RC ECO:0000313|Proteomes:UP000288587};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT83870.1}.
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DR EMBL; SACM01000004; RVT83870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2WNC1; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000288587; 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:2001070; F:starch binding; IEA:InterPro.
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 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; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
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 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; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 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 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:UP000288587}.
FT DOMAIN 501..612
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 612 AA; 65038 MW; D2E6E6180C76A600 CRC64;
MAAFGLAAAS LPASALNPRD TSVQLFQWSW NDIATECQQW LGPKGFGAVQ ISPPHASKVA
GGWWGVYQPV NYVNLTSRMG NEAQLRSMVT ACKNAGVRVY ADVVVNQMAD GTGTATDGSA
FNGTTLSYPF FSGNDFNPNC TIEGSDYNSP ATVDRVRNCR LGGLPDLATQ NAYVQGQITN
YLVKLLQLGV DGFRIDAAKH MPPTALAQII SAVKARQPKT LAGEEIWITQ EIIPDGATNR
ADYAGIGTIN EFKYTYLMRD AFRNANGQNL ASIPAAMGSW GNWGGAWGFL PPQQATVFLN
NWDTERHSGD SLNASNYIAG QTNDTQGTAR YDLANVFMLA QGYGEAQVQS GYRFSNKDAD
RPTVSPYSNG VAQINVVWDF VHRWRPVSNM VKFRSVTNGQ PITNWTTGTG SQVAFSRGTK
GFVALNNSAS AWSRSFATGL PAGTYCNVLT GERNAAGTGC TGDSVTVSSS GTATLNIPAD
GGGAFPGVAL HEGQRLSSVQ PPPVGTCAVT FTIANANTVW GENVHIAGNQ GALGNWAPAS
APKLNIQGST ANSPWTLTVA LPAATAVQYK YIKRNGTATR WEGDQATTSL NREFTTCAAG
GAMSRNDGSF KF
//
