IPUA_ASPNG
ID IPUA_ASPNG Reviewed; 564 AA.
AC O00105;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Isopullulanase;
DE EC=3.2.1.57;
DE Flags: Precursor;
GN Name=ipuA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9642 / CBS 246.65 / DSM 63263 / NBRC 6342 / NRRL 3536;
RX PubMed=9169610; DOI=10.1042/bj3230757;
RA Aoki H., Yopi X., Sakano Y.;
RT "Molecular cloning and heterologous expression of the isopullulanase gene
RT from Aspergillus niger ATCC 9642.";
RL Biochem. J. 323:757-764(1997).
RN [2]
RP PROTEIN SEQUENCE OF 20-29, AND CHARACTERIZATION.
RC STRAIN=ATCC 9642 / CBS 246.65 / DSM 63263 / NBRC 6342 / NRRL 3536;
RX PubMed=8987855; DOI=10.1271/bbb.60.1795;
RA Aoki H., Yopi X., Padmajanti A., Sakano Y.;
RT "Two components of cell-bound isopullulanase from Aspergillus niger ATCC
RT 9642 -- their purification and enzymatic properties.";
RL Biosci. Biotechnol. Biochem. 60:1795-1798(1996).
CC -!- FUNCTION: Hydrolyzes pullulan, a linear polymer which is composed of
CC maltotriose units with alpha-1,6 glucosidic linkages, to produce
CC isopanose (Glca1-4Glca1-6Glc).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of pullulan to isopanose (6-alpha-
CC maltosylglucose).; EC=3.2.1.57;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated.
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DR EMBL; AB001940; BAA19473.1; -; Genomic_DNA.
DR EMBL; D85240; BAA18971.1; -; Genomic_DNA.
DR PDB; 1WMR; X-ray; 2.40 A; A/B=20-564.
DR PDB; 1X0C; X-ray; 1.70 A; A/B=20-564.
DR PDB; 2Z8G; X-ray; 1.70 A; A/B=20-564.
DR PDB; 3WWG; X-ray; 2.20 A; A/B/C/D=20-564.
DR PDBsum; 1WMR; -.
DR PDBsum; 1X0C; -.
DR PDBsum; 2Z8G; -.
DR PDBsum; 3WWG; -.
DR AlphaFoldDB; O00105; -.
DR SMR; O00105; -.
DR CAZy; GH49; Glycoside Hydrolase Family 49.
DR CLAE; IPU49A_ASPNG; -.
DR BRENDA; 3.2.1.57; 518.
DR EvolutionaryTrace; O00105; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051675; F:isopullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR Gene3D; 2.60.350.10; -; 1.
DR InterPro; IPR041402; B_solenoid_dext.
DR InterPro; IPR035953; Dextranase_N-ter.
DR InterPro; IPR005192; Glyco_hydro_49_C.
DR InterPro; IPR023226; Glyco_hydro_49_N_dom.
DR InterPro; IPR041274; IPU_b_solenoid.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF18841; B_solenoid_dext; 1.
DR Pfam; PF03718; Glyco_hydro_49; 1.
DR Pfam; PF17433; Glyco_hydro_49N; 1.
DR Pfam; PF18783; IPU_b_solenoid; 1.
DR SUPFAM; SSF101596; SSF101596; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Glycosidase;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8987855"
FT CHAIN 20..564
FT /note="Isopullulanase"
FT /id="PRO_0000021520"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 170..182
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 335..345
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2Z8G"
FT STRAND 362..372
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 379..391
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 407..419
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 452..472
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 481..497
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 523..533
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 540..547
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:1X0C"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:1X0C"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1X0C"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:1X0C"
SQ SEQUENCE 564 AA; 61449 MW; B6C0B70BF737CC40 CRC64;
MRSTGYLLTL SAAFQVAQAA VTANNSQLLT WWHNTGEINT QTPVADGNVR QSGLYSVKVQ
TTPASSSLYY DSFVYLAIPG NGMSDQLQYT QGYNQTQAWT SFLYSHDATV KISRNGSSAN
SNVVIRPTSL NFPVRYDNQS VYITVPYSPT GYRFSVEFDD DLISLAPSGA RQPENALLIF
ASPFENSSTK PQPGSPNSIA PAPGRVLGLN TTSASTVVFN PGVYYFTGHD HMVLSSSVTW
VYFAPGAYVK GAVEFLSTAS EVKASGHGVL SGEQYVWYAD PDEGYQKASG ANNNGLRMWR
GTLGNSSQTF VLNGVTVSAP PFNSMDWSGN SLDLITCRVD DYKQVGAFYG QTDGLEMYPG
TILQDVFYHT DDDGLKMYYS NVTARNIVMW KESVAPVVEF GWTPRNTENV LFDNVDVIHQ
AYANAGNNPG IFGAVNNYLY APDGLSSNHS TGNSNMTVRN ITWSNFRAEG SSSALFRINP
IQNLDNISIK NVSIESFEPL SINTTESWMP VWYDLNNGKQ ITVTDFSIEG FTVGNTTITA
SNAASVGRID GVDPAYAGSV HYID
