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Database: UniProt
Entry: W4DY48_9BACL
LinkDB: W4DY48_9BACL
Original site: W4DY48_9BACL 
ID   W4DY48_9BACL            Unreviewed;       999 AA.
AC   W4DY48;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Alpha amylase, catalytic domain protein {ECO:0000313|EMBL:ETT72516.1};
GN   ORFNames=C173_13416 {ECO:0000313|EMBL:ETT72516.1};
OS   Paenibacillus sp. FSL R7-277.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT72516.1, ECO:0000313|Proteomes:UP000019051};
RN   [1] {ECO:0000313|EMBL:ETT72516.1, ECO:0000313|Proteomes:UP000019051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT72516.1,
RC   ECO:0000313|Proteomes:UP000019051};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT72516.1}.
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DR   EMBL; ASPX01000035; ETT72516.1; -; Genomic_DNA.
DR   RefSeq; WP_036725572.1; NZ_ASPX01000035.1.
DR   AlphaFoldDB; W4DY48; -.
DR   PATRIC; fig|1227352.4.peg.2689; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG2819; Bacteria.
DR   eggNOG; COG4733; Bacteria.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000019051; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
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:InterPro.
DR   CDD; cd00063; FN3; 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; 4.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
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; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF03423; CBM_25; 2.
DR   Pfam; PF00041; fn3; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SMART; SM01066; CBM_25; 2.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
FT   DOMAIN          564..649
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          892..998
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          772..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   999 AA;  106409 MW;  76A1BC2C4016CBA5 CRC64;
     MKRKRNRLLV PVLIASIVLS IMMNLFVLPP AKVEAASIGT VTENDTIYQI MVDRFHDGDS
     SNNATGAAIR YGENSEEDFR YMKGGDWQGV IDKLPYIHNM GYTAIWISPV AEPQMTNREN
     NGTGKNTAYH GYNVKDPNKA NPYFGTKEKL KELVDSAHAL GIKVIIDVVP NHIGDYMLGT
     QAYYDIPSLQ PAAPFNNPAW YHHNGDINWS LADGRYDQWA QDYLENHDLG GLDDIDFDVP
     VAKQAIFSSI KGWFDYTEAD GARVDAAKLM KPTDIGELQN LLGVNTFGEN FDGNAEFVSR
     WVGQNKEWGM LDFPLFFSVL NSFAYGQSFD ANIKGTLAQD SYYGGNANHM VTFIDNHDRN
     RFLTEAGGSV EKLQNALSFI FTVRGTPVVF QGTEQNKGNG NGQIMTGGIA DTWNRWSMVK
     RDASGNVLEN YFNENASTFK HVAKLNEIRK NNPALRTGTQ REMWSAQNLY AFSRRIDSGT
     NVGQEVISAF SNASGGSQTV TLPLRAESTL TAGTVLVNQL NPSDTVTVQA GGVTGKQITI
     TLGANSAKIY AKTQPVTDTQ APSVPGNVTA TVQNASSALV SWSASTDNVG VTGYEIYRNG
     VKIGTSATTS FTDNGLVGST NYSYTVKAYD AAMNLSAFSA AALIVTPAGN SVTIYYKQGY
     TNPYIHYRPV GGTWTTSPGV AIPAAEVAGY NKITINIGAA TQLEACFNNG SGTWDSNGGS
     NYLFGTGTWT YTPTGNIQAG GPVTPTATPT VAPTATPTVT PTVAPTVAPT ATPTVAPSAT
     PTASPTVAPT ATPVPTATPA GNTATIYYKN TAFSNSYIHY KLDGATTWTT SPGVQMQAST
     FSGYKAITIP LGSATGLTAA FNNGSGTWDN NGGNNYHFGT GSSSLVGGSL TSGEPQADSV
     TFRVSVPGST PANAPVYLTG SFNSWNAADA AYLLTRGSDG VYSITLNLPA GSAVTYKLTR
     GSWGTVETVS SGADIANRTL TPAGGAQTVT LSVQRWKDQ
//
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