NEPU_GEOSE
ID NEPU_GEOSE Reviewed; 588 AA.
AC P38940;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Neopullulanase;
DE EC=3.2.1.135;
GN Name=nplT;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5.
RC STRAIN=TRS40;
RX PubMed=2482332; DOI=10.1099/00221287-135-6-1521;
RA Kuriki T., Imanaka T.;
RT "Nucleotide sequence of the neopullulanase gene from Bacillus
RT stearothermophilus.";
RL J. Gen. Microbiol. 135:1521-1528(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CALCIUM AND GLUCOSE,
RP COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=12547200; DOI=10.1016/s0022-2836(02)01402-x;
RA Hondoh H., Kuriki T., Matsuura Y.;
RT "Three-dimensional structure and substrate binding of Bacillus
RT stearothermophilus neopullulanase.";
RL J. Mol. Biol. 326:177-188(2003).
CC -!- FUNCTION: Hydrolyzes pullulan efficiently but only a small amount of
CC starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to
CC form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form
CC maltotriose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).;
CC EC=3.2.1.135;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12547200};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12547200};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12547200}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M28138; AAA22622.1; -; Genomic_DNA.
DR PIR; A37008; A37008.
DR PDB; 1J0H; X-ray; 1.90 A; A/B=1-588.
DR PDB; 1J0I; X-ray; 2.40 A; A/B=1-588.
DR PDB; 1J0J; X-ray; 2.80 A; A/B=1-588.
DR PDB; 1J0K; X-ray; 3.20 A; A/B=1-588.
DR PDBsum; 1J0H; -.
DR PDBsum; 1J0I; -.
DR PDBsum; 1J0J; -.
DR PDBsum; 1J0K; -.
DR AlphaFoldDB; P38940; -.
DR SMR; P38940; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ag:AAA22622; -.
DR BRENDA; 3.2.1.135; 623.
DR EvolutionaryTrace; P38940; -.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0031216; F:neopullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
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; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Glycosidase; Hydrolase;
KW Metal-binding.
FT CHAIN 1..588
FT /note="Neopullulanase"
FT /id="PRO_0000054310"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12547200"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12547200"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12547200,
FT ECO:0007744|PDB:1J0H"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12547200,
FT ECO:0007744|PDB:1J0H"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12547200,
FT ECO:0007744|PDB:1J0H"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12547200,
FT ECO:0007744|PDB:1J0H"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12547200,
FT ECO:0007744|PDB:1J0H"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12547200"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12547200"
FT BINDING 423..424
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12547200"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12547200"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12547200"
FT SITE 424
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1J0I"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 303..320
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1J0K"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1J0K"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 484..499
FT /evidence="ECO:0007829|PDB:1J0H"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:1J0H"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:1J0H"
FT STRAND 580..587
FT /evidence="ECO:0007829|PDB:1J0H"
SQ SEQUENCE 588 AA; 69145 MW; B2C7195D1CE34A33 CRC64;
MRKEAIYHRP ADNFAYAYDS ETLHLRLRTK KDDIDRVELL HGDPYDWQNG AWQFQMMPMR
KTGSDELFDY WFAEVKPPYR RLRYGFVLYS GEEKLVYTEK GFYFEVPTDD TAYYFCFPFL
HRVDLFEAPD WVKDTVWYQI FPERFANGNP SISPEGSRPW GSEDPTPTSF FGGDLQGIID
HLDYLVDLGI TGIYLTPIFR SPSNHKYDTA DYFEVDPHFG DKETLKTLID RCHEKGIRVM
LDAVFNHCGY EFAPFQDVWK NGESSKYKDW FHIHEFPLQT EPRPNYDTFR FVPQMPKLNT
ANPEVKRYLL DVATYWIREF DIDGWRLDVA NEIDHEFWRE FRQEVKALKP DVYILGEIWH
DAMPWLRGDQ FDAVMNYPFT DGVLRFFAKE EISARQFANQ MMHVLHSYPN NVNEAAFNLL
GSHDTSRILT VCGGDIRKVK LLFLFQLTFT GSPCIYYGDE IGMTGGNDPE CRKCMVWDPM
QQNKELHQHV KQLIALRKQY RSLRRGEISF LHADDEMNYL IYKKTDGDET VLVIINRSDQ
KADIPIPLDA RGTWLVNLLT GERFAAEAET LCTSLPPYGF VLYAIEHW
