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 22-FEB-2023, entry version 98. 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. 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; 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 GlyCosmos; O00105; 15 sites, No reported glycans. 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; 2.60.350.10; Dextranase, N-terminal; 1. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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; Dextranase, N-terminal domain; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 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 //