AMYB_PAEPO
ID AMYB_PAEPO Reviewed; 1196 AA.
AC P21543;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Beta/alpha-amylase;
DE Includes:
DE RecName: Full=Beta-amylase;
DE EC=3.2.1.2;
DE Includes:
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1;
DE Flags: Precursor;
OS Paenibacillus polymyxa (Bacillus polymyxa).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-936, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=72;
RX PubMed=2435707; DOI=10.1128/jb.169.4.1564-1570.1987;
RA Kawazu T., Nakanishi Y., Uozumi N., Sasaki T., Yamagata H., Tsukagoshi N.,
RA Udaka S.;
RT "Cloning and nucleotide sequence of the gene coding for enzymatically
RT active fragments of the Bacillus polymyxa beta-amylase.";
RL J. Bacteriol. 169:1564-1570(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 689-1196, AND PARTIAL PROTEIN
RP SEQUENCE.
RC STRAIN=72;
RX PubMed=2464578; DOI=10.1128/jb.171.1.375-382.1989;
RA Uozumi N., Sakurai K., Sasaki T., Takekawa S., Yamagata H., Tsukagoshi N.,
RA Udaka S.;
RT "A single gene directs synthesis of a precursor protein with beta- and
RT alpha-amylase activities in Bacillus polymyxa.";
RL J. Bacteriol. 171:375-382(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776.
RC STRAIN=ATCC 8523 / DSM 356 / CCM 1465 / CIP A45 / VKM B-418;
RX PubMed=2438660; DOI=10.1093/nar/15.9.3934;
RA Rhodes C., Strasser J., Friedberg F.;
RT "Sequence of an active fragment of B. polymyxa beta amylase.";
RL Nucleic Acids Res. 15:3934-3934(1987).
RN [4]
RP DISULFIDE BOND, AND MUTAGENESIS OF CYSTEINE RESIDUES.
RX PubMed=1827035; DOI=10.1021/bi00232a033;
RA Uozumi N., Matsuda T., Tsukagoshi N., Udaka S.;
RT "Structural and functional roles of cysteine residues of Bacillus polymyxa
RT beta-amylase.";
RL Biochemistry 30:4594-4599(1991).
CC -!- FUNCTION: The precursor protein is proteolytically cleaved to produce
CC multiform beta-amylases and a 48 kDa alpha-amylase after secretion.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
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;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P36924};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P36924};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC hydrolase 14 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M15817; AAA85446.1; -; Genomic_DNA.
DR EMBL; Y00150; CAA68344.1; -; Other_DNA.
DR PIR; A29130; A29130.
DR PDB; 2LAA; NMR; -; A=455-558.
DR PDB; 2LAB; NMR; -; A=565-668.
DR PDB; 3VOC; X-ray; 1.95 A; A=36-454.
DR PDBsum; 2LAA; -.
DR PDBsum; 2LAB; -.
DR PDBsum; 3VOC; -.
DR AlphaFoldDB; P21543; -.
DR BMRB; P21543; -.
DR SMR; P21543; -.
DR STRING; 1052684.PPM_4861; -.
DR CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1874; Bacteria.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR000125; Glyco_hydro_14A_bac.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03423; CBM_25; 2.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00841; GLHYDLASE14A.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01066; CBM_25; 2.
DR SUPFAM; SSF51445; SSF51445; 2.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Polysaccharide degradation; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..35
FT CHAIN 36..1196
FT /note="Beta/alpha-amylase"
FT /id="PRO_0000001457"
FT REPEAT 455..558
FT REPEAT 565..668
FT REGION 36..454
FT /note="Beta-amylase"
FT REGION 544..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..1196
FT /note="Alpha-amylase"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 395..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36924"
FT DISULFID 118..126
FT /evidence="ECO:0000269|PubMed:1827035"
FT MUTAGEN 118
FT /note="C->S: 5-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:1827035"
FT MUTAGEN 126
FT /note="C->V: 20-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:1827035"
FT MUTAGEN 358
FT /note="C->S: 60-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:1827035"
FT CONFLICT 1
FT /note="M -> MIGL (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="N -> S (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="N -> D (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> N (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> Q (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="NA -> KS (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="G -> S (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="N -> S (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="D -> A (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="S -> L (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="A -> T (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="A -> T (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="D -> N (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="T -> A (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 725..728
FT /note="AFTS -> VFSP (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="N -> K (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="N -> S (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="S -> N (in Ref. 3; CAA68344)"
FT /evidence="ECO:0000305"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3VOC"
FT TURN 264..269
FT /evidence="ECO:0007829|PDB:3VOC"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 275..303
FT /evidence="ECO:0007829|PDB:3VOC"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3VOC"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 373..387
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 402..413
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:3VOC"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:3VOC"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2LAA"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:2LAA"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:2LAA"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 605..615
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:2LAB"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:2LAB"
SQ SEQUENCE 1196 AA; 130893 MW; A41EA6B70F257064 CRC64;
MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA KINDWGSFKK
QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN AVKEAGLKWV PIISTHKCGG
NVGDDCNIPL PSWLSSKGSA DEMQFKDESG YANSEALSPL WSGTGKQYDE LYASFAENFA
GYKSIIPKIY LSGGPSGELR YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL
DKINAAWGTK LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH
KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA DLDLTFTCLE
MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG GSGFQKIEEK ITKFGYHGFT
LLRINNLVNN DGSPTGELSG FKQYIISKAK PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG
GSWTAAPGVK MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY
TPGNSGNAGT ITSGAPAGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK
MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY TPGSNGAAGT
IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ TEKLSGVSLN VSTSTYAPNS NGVEVTAQTE
APSGAFTSMD LGTLSNPTSL NTDWSKQSIY FIMTDRFSNG DPSNDNYGGF NSNNSDQRKW
HGGDFQGIIN KLDYIKNMGF TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKLQE
LVRKAHDKNI AVMVDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITDG DYNSNNQWKI
ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF LKDFDQAANT
FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD QSMRKIKDRY SDDRYYRDAQ
TNGVFIDNHD VKRFLNDASG KPGANYDKWP QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD
DPANRENMNF NANHDLYQYI AKLNYVRNNH PALQNGSQRE KWVDDSFYSF QRSKNGDEAI
VFINNSWNSQ TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKVFTK
