ID A0RAZ2_BACAH Unreviewed; 451 AA.
AC A0RAZ2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Alpha-amylase family protein {ECO:0000313|EMBL:ABK84385.1};
GN OrderedLocusNames=BALH_1021 {ECO:0000313|EMBL:ABK84385.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK84385.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK84385.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK84385.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP000485; ABK84385.1; -; Genomic_DNA.
DR RefSeq; WP_011732615.1; NC_008600.1.
DR AlphaFoldDB; A0RAZ2; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; btl:BALH_1021; -.
DR HOGENOM; CLU_006462_7_3_9; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..330
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 451 AA; 52680 MW; 4AFF40EABF14DA5E CRC64;
MRFVRIIGII FLQLKTWGMR VGKIHTRKLF ICFCLAVVLF VPIHTFADEK REWRDEVIYS
IMIDRFNNGE PKNDKQLEVG NLEGYQGGDI RGIIKRLDYI KEMGFTTVML SPLFESVKYD
GLDVRNFQKV NEHFGTENDV KELVQEAHAK GMKVIFQFPL GENEQQVIDS MKWWVKEVDL
DASYVMHSEK KSPAFWDDVQ KDMQVIKKDF RVMTKEDSEY NEKIVESFSK ADVSVKSLYD
VSKKDEEFIT FLDNQDTKRF ARIAKENMNY PPSRLKLALT YLLTSPGIPN FYYGTEIALD
GGDTPDNRRL MDFKSDEKFM QHITKLGELR QTRPSLRRGT FELLYDKNGM SVLKRKYKGE
VTLVAINNTK ETQKVALPAS AIGEKQELRG LLEDEIIREE NRKFYLVLKR EESNVYKVNR
ETGVNWLFIS LIVGVNVLFI TFLIAVKKRR K
//
