ID H3A6W9_LATCH Unreviewed; 515 AA.
AC H3A6W9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN Name=LOC102365271 {ECO:0000313|Ensembl:ENSLACP00000005390.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000005390.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000005390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AFYH01189169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A6W9; -.
DR STRING; 7897.ENSLACP00000005390; -.
DR Ensembl; ENSLACT00000005438.1; ENSLACP00000005390.1; ENSLACG00000004795.1.
DR eggNOG; KOG2212; Eukaryota.
DR GeneTree; ENSGT00940000154802; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; H3A6W9; -.
DR OMA; TWVETHD; -.
DR TreeFam; TF312850; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000004795; Expressed in chordate pharynx and 6 other cell types or tissues.
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 Chloride {ECO:0000256|ARBA:ARBA00023214};
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:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..515
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003579635"
FT DOMAIN 30..418
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 427..515
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 515 AA; 58370 MW; 063A80A8ED0E7506 CRC64;
MSEDMRILTL LAVLGVCWAQ YNPNTQPHKT AIVHLFEWRW VDIAAECERY LAPNGFGGVQ
ISPPNDHIVL NNPWMPWYER YQPISYKLCS RSGTENEFVD MVTRCNNVGV YIYADAVINH
MCGASGGAGT HSSCGTYFNA GTEDFPAVPY SSWEFNDGKC KTKSGEIESY QDANQVRDCR
LVSLLDLNLQ KDYVRGKIAE YMNRLIRIGV AGFRVDGSKH MWPGDMKAVF DQLNSLNTRW
FPKDSKPFIY QEVIDLGGEP IKSSDYFGNG RVTEFKYGAK LGYVIRKWNG EKMAYLKNWG
EGWSFMPSDK AVVFVDNHDT QRGHGPGGAS VLTFWNSRMY KIAVGFMLAH PYGFTRVMSS
FRWPRHFVNG KDTNDWIGPP SYSDGTTKRV TINPDTTCGN DWVCEHRWRQ IKNMVMFRNV
VDGQPFSNWW DNGSNQIAFG RGNKGFIIFN NDDWYMDVTL QTGLPAGTYC DVISGQMENG
ACTAVQIQVN DDGRANFKIS NTAEDPFIAI HTKPT
//
