ID A0A0Q9MDQ3_9BACL Unreviewed; 2086 AA.
AC A0A0Q9MDQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:KRE64173.1};
GN ORFNames=ASL11_23405 {ECO:0000313|EMBL:KRE64173.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE64173.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE64173.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE64173.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE64173.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE64173.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KRE64173.1}.
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DR EMBL; LMSD01000025; KRE64173.1; -; Genomic_DNA.
DR RefSeq; WP_056620380.1; NZ_LMSD01000025.1.
DR STRING; 1736398.ASL11_23405; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11338; AmyAc_CMD; 1.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF234; INTRACELLULAR MALTOGENIC AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1901..1961
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1962..2025
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2029..2086
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 463..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1693..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2086 AA; 225922 MW; 24E9DED719BECBBC CRC64;
MGLWHRKRGT QLLSALSALL LIVQLFTGLF AGSTRVLAAA DQITEQPGGK SKWVVVGSFQ
GWDNASTDTR MKHLVGEFYA FTKELPAGSY EFKIVKSGSW DGYSNNSNNF SFSLGETTKV
NFYVNDEIGQ ARISLPGVAG IQQYMPALGL NEQPRLVGSI QPLFGEAEWS PDGANQMFVD
YRFNNTVYKL QRHIPVGSYE AKIVFGQNWD APNYGTATGA NVKIATVDEA DVTFTFDNSA
QTKALTHDYV AKDGAFDGQI KKDSLFFDSR SVTYKKPFGA IPAGGQDVTL RMAAAKGDLQ
TAKAELTAPD GSSNAYLMKK VTAVADKEYW EVTVPAADFA GKVGIWGYKF IVVDGSSKAE
YGDDSSRGGS GSVADEGAVP YDLTVYAPDY KTPDWMKNAV VYQIFPDRFF DGSKDNNRAK
TVDGARGVID PKYGTSKNGQ QLQYFDGGVP NDPTPAQVWG GTSIVPENPD RTKPENKPYY
PNAKTDGAWT NEFYGGDVQG IEQKLGYLKS LGITAVYLNP VSWAASNHKY DATDYKHLDP
MFGQPVYNTS GDPASGLDYV KTREASDQVF ENFTKAARTA GIKVINDGVF NHVGDDSIYF
DRYDKYPEIG AYEYWAAVYD KMNAASITQE QAEADVRALF TSQINPMTGQ NYKWPDDFRY
VSWFTVTNDK VKDRDDDNLH YKYDAWWGYD SLPVMDAKDP QTAPTVYLPT DTLFLPGQHE
WNNIHYRDNV IGHSLTGLTE TDAQKAMQFA NSQRWLWMGT SGWRLDVAPD VSAGTWGKFR
EAVKSAAGRT NVNGTVIDEP VIIGEEWGVA TKFLLGDQFD SVMNYRFRGA LQSFLSGGNA
DTFNQALESI REDYPKEAWE ALMNLVDSHD TTRSITKYDH PEWEEEHLVI APEASTNAKK
LQELTAIFQM GYPGAPTIYY GDEVGLTGTK DPDSRRFFPW ERVVANGDGT FSGTGDYQNL
LSVYQKAAKV RGDNAVFRTG DLKAVYSQGN VIAYARKNDS RGALLVVNRG ANPQSIEVDV
AGFLPDGLAL TDQLYGSTKA VVASGKISLT VPALTGFMMV SDDELQAVPQ VTGVQAQGDK
GKVMLSWNSV SGAESYQIYR AAIEGGAVQL VGSTADLNHL DVNVVNGTKY YYAVTARIGS
GESFFSDMVA ATPAFQIASL GTPSTVTDNV YAGVGKATGR ITVNVNIPGL TDDAALAGKE
APNLLARLGF YKEGTDPAAA QDTKFRYDSD QSGSKMYWGS FEPTEAGVYN YFAKVSTDNG
EHYTQSDTVT LEVYGDPNDT TAPAAPALNS IAVESNRSYL KWTASDSSIA GFDVYRQSVT
DATYQKIATL AATAIDYTDY AVSNDVLYTY QVAAFDQSYN RAFSEKQSVT PKLVMVDVLM
RLHLPDYTPT SDDINIAGSF NGWNASSTKL HVPSGATDRG VVEYSFKMMA GKSIEYKYTR
GTWETEAFTS HTRTPGDTAD YGNWAYSSTV TNMKLTIKND GGNQMVVNDY VLRWVDMPMI
LTMPRITYGS NVAYSTEESS FKLKGVVPYG VNFSINGQPI PQNSMDAAGN VELDAIPLAL
GSNHFELHIE PTPETLLLPW YEDKGRAGQA TKTITLDITR TSGGSAQEPV LNQLQWSEVN
TALTVGDTRQ LQVLGEYSDD SKKSLTGVEF TSSNTNIADV TPEGLVTAKS QGEVKITASF
GGKTAEITLN ISSAPSNEGS GGDTMATTPA DKPSTTKQID EAALTNGKDG KVGIELSSGE
REVKLPVNAA ELLGSKTLEI KQGGISIEVP SSLLKALAIL IPGGSSEGAQ LSLAVNTVGA
EAAQKLINQG AASTGAIIKP VSTVYDFTLS ALTKDGKTLK LPTFDQPVTL TFHVQDGANI
PLSGVYYVSD AGELTYIGGT WENGGLTAKV FHFSKYAVLE YNKSFNDLPA AHWAANAVRE
LAAKHVVEGI TDAAFAPERE VTRAEFSAML VRALNLSAKG EASLPFSDVP GSAWYSTVVA
IAYSNGIVSG RGSSTFAPDA PITRQEMAAM VVRAYGVHTG TNAPAADIPV GFDDAAGIAP
WAVNFVQSAV GLKLMQGRGE REFAPVGITT RTECAQVLLN LLHSGK
//
