ID I3INY2_9BACT Unreviewed; 575 AA.
AC I3INY2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=KSU1_D0118 {ECO:0000313|EMBL:GAB63427.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB63427.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB63427.1, ECO:0000313|Proteomes:UP000002985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA Furukawa K., Fujii T.;
RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT reductase instead of a NirS-type with cytochrome cd1.";
RL FEBS Lett. 586:1658-1663(2012).
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|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:GAB63427.1}.
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DR EMBL; BAFH01000004; GAB63427.1; -; Genomic_DNA.
DR AlphaFoldDB; I3INY2; -.
DR STRING; 247490.KSU1_D0118; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000002985; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000002985}.
FT DOMAIN 33..464
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 575 AA; 65827 MW; 3F8B3305411FE231 CRC64;
MAERITSIKE LDFTPQEKAF PSPGDWRDLF IYFLLADRFD DNKENIPAYD PASAPRGRDP
EQGGVFQGGN IKGIIRRLDY IRGLGANAIW LSPVLKNRQE RMDSYHGYGI QDFLEVDPRF
GTKQDLQELV RQAHKKGMYV ILDIIINHTG DNWAYPGDYP YYYWREAPGP FDFGFWREAD
STPGFQKGDA VWPQELQHQG YYKRRGQIRD WNDPDEAVHG DFVSLKELDI AQPEVLDTLI
KAYKYWIAVA DIDGFRVDTV KHIENSATAI FCNAVREYAK RIGKQNFFLF GEVVADDPTL
ERYIGRNSRI EGTNERFPSL DACLDFPLYF MLEEVIKGLA NPSGLRERYE RFRTMYADHG
AAGQYFVTFV DNHDQMARPY RRFMHGNPHP KQAVLALGYL LTSQGVPCMY YGTEQGFDGG
GDNDRYIREC MFGGQWGAFD STGRHFFNKN HPIYQGIAGI ASVRQREPAL RYGRQYFREI
SGNGVDFGYP IDGKCVLAYS RILDDCEILI ALNLDASPRN DFITIDINLN PAGQKMVNLL
APEKQVTVEQ RGQRHAVKVP LDGHELVILK RSGSF
//
