AAMY_NIACI
ID AAMY_NIACI Reviewed; 1290 AA.
AC A0P8X0;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Alpha-amylase {ECO:0000303|PubMed:17090949};
DE EC=3.2.1.1 {ECO:0000269|PubMed:17090949};
DE Flags: Precursor;
GN Name=igtZ {ECO:0000303|PubMed:17090949};
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-37, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=AM7;
RX PubMed=17090949; DOI=10.1271/bbb.60294;
RA Watanabe H., Nishimoto T., Kubota M., Chaen H., Fukuda S.;
RT "Cloning, sequencing, and expression of the genes encoding an
RT isocyclomaltooligosaccharide glucanotransferase and an alpha-amylase from a
RT Bacillus circulans strain.";
RL Biosci. Biotechnol. Biochem. 70:2690-2702(2006).
RN [2]
RP 3D-STRUCTURE MODELING, AND ACTIVE SITE.
RX PubMed=22819817; DOI=10.1016/j.febslet.2012.07.020;
RA Janecek S., Kuchtova A.;
RT "In silico identification of catalytic residues and domain fold of the
RT family GH119 sharing the catalytic machinery with the alpha-amylase family
RT GH57.";
RL FEBS Lett. 586:3360-3366(2012).
CC -!- FUNCTION: Acts on maltooligosaccharides that have a degree of
CC polymerization (DP) of 4 or more, amylose, and soluble or raw starch to
CC produce glucose and maltooligosaccharides up to DP5 by a hydrolysis
CC reaction. Also acts on maltooligosyl trehaloses that have DP5 or more
CC to produce trehalose as the major hydrolysis product.
CC {ECO:0000269|PubMed:17090949}.
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:0000269|PubMed:17090949};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:17090949};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:17090949};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 119 (GH119) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB248273; BAF37284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0P8X0; -.
DR SMR; A0P8X0; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR CAZy; GH119; Glycoside Hydrolase Family 119.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 4.
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; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF03423; CBM_25; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM01066; CBM_25; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:17090949"
FT CHAIN 32..1290
FT /note="Alpha-amylase"
FT /id="PRO_0000432229"
FT DOMAIN 817..902
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1183..1289
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 902..978
FT /note="CBM25"
FT /evidence="ECO:0000255"
FT REGION 994..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1171
FT /note="CBM25"
FT /evidence="ECO:0000255"
FT COMPBIAS 1005..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:22819817"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:22819817"
SQ SEQUENCE 1290 AA; 138787 MW; D205B76690E68198 CRC64;
MTRKTRYLHQ ITTLILGGLL IVPAAAPPVS ADIAATHVYH NHMPNFWAYY DLNTYNSTPV
GSPIRYTYDG EVIQLKQNPP AGYPYYLPNG SPMPHDDLVS YYSHHAKTGA YLTWPWSVAN
TLHSSHPQAQ MHVTMSGSVV NNVNSIIQQG NVSGYNNPAW GTPWKNAVTQ LKTAGGDNRL
DLIHFSGHHS MGPLVGNDYL LKDMIYHGAT MAQPYFLGSS YKSSKGFFPT ELGFSERIIP
VLNKLGIQWS VIGNNHFSRT LKDYPLLDSP GTDTMISPPN RSDLQNVSTA GAWVNEPMFN
EQQVVYNKYP FASTAHWVRY VDPATGAESR VVGVPVAQAQ SWEEGYLGQV KADALKPYEN
LVAQKQIFVV AHDGDNSSGR AGSEETWRNA GNVTYADSGV TGMGIDEYLR SNTPAAADVV
HVQDGSWIDT RDSSSDPAWY HWHLPFGIWK GQFAAFNQVN GTAYAPKKNL AGVEEGMTVS
FEKGYHYLER NFALLQASLN YAKTAEQIWL EEHPNYWKPA NPLDREVTYE GNQLNPWMLS
YPVKGNPAND YAGGANPAEL AWYFLLPAMD SGFGYYDENV DDSVKPALSF NQSLYFSKPY
VSQKLAKDKT GPSVWWPQRY PYNPGSANVS KAEGWTLQHY NNAFAIYTYA FDTSGISEIK
VKVRAHRDKT ADAADNTFKV YDPAGLAAAG IANIDPAKVG AWTEYPMNVR DLSADINGVD
WQPSSMTIMQ KVPATDIGNL YFSYISDYRD QLLDYFIEAK DAKGNVTQSD IQQVYVGAGK
YKLANGKYTE SMQGTIEGTH PFITDVPAVP DTEAPAVPAN LQATVMNASS VGLSWNAATD
NIRVTGYEIY RNGVRIGTTP STSYTDSGLS ASTAYEYRVK AYDASGNLSG FSAAATATTP
AGNHVTVYYK QGYSTPYIHY RPAGGTWTTA PGVAIPAAEV AGYNKITINI GAATQLEACF
NNGSGTWDSN GGSNYLFGTG TWTYTPTGKI QAGAPVAPSA TPTVAPTATP TPKPSVTPTV
TPITTPTVAP TLSPTPTVAP TVKPSATPIA TPTVTPTVSP TATPTVVPTI APTATPTTSP
SATPVPTATP AGNSATIYYK NTAFSNSYIH YKLDGATAWT TSPGVQMQAS TFSGYKAITI
PLGSATGLTA AFNNGSGIWD NNGGSNYHFG TGSSSLTGGN LITGEPQADS VTFRVSVPGS
TPANAPVYLT GSFNSWNAAD PAYLLTRGSD GIYSITLNLP AGSAVTYKLT RGSWATVETA
SSGADITNRT LTPAGGAQTV TLTVQRWKDQ
