ID MANA_ASPNC Reviewed; 383 AA. AC A2QKT4; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Probable mannan endo-1,4-beta-mannosidase A; DE EC=3.2.1.78; DE AltName: Full=Endo-beta-1,4-mannanase A; DE Flags: Precursor; GN Name=manA; Synonyms=man1; ORFNames=An05g01320; OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of CC seed galactomannans and wood galactoglucomannans. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in CC mannans, galactomannans and glucomannans.; EC=3.2.1.78; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. 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; AM270105; CAK96471.1; -; Genomic_DNA. DR RefSeq; XP_001390707.1; XM_001390670.1. DR PDB; 3WH9; X-ray; 1.57 A; A/B=39-383. DR PDBsum; 3WH9; -. DR AlphaFoldDB; A2QKT4; -. DR SMR; A2QKT4; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR GlyCosmos; A2QKT4; 3 sites, No reported glycans. DR EnsemblFungi; CAK96471; CAK96471; An05g01320. DR GeneID; 4980871; -. DR KEGG; ang:An05g01320; -. DR VEuPathDB; FungiDB:An05g01320; -. DR HOGENOM; CLU_031603_4_1_1; -. DR OrthoDB; 2717493at2759; -. DR BRENDA; 3.2.1.78; 518. DR Proteomes; UP000006706; Chromosome 7L. DR GO; GO:0005576; C:extracellular region; IDA:AspGD. DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:AspGD. DR GO; GO:0046355; P:mannan catabolic process; IDA:AspGD. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR045053; MAN-like. DR PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1. DR PANTHER; PTHR31451:SF67; MANNAN ENDO-1,4-BETA-MANNOSIDASE A-RELATED; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase; KW Hydrolase; Reference proteome; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..383 FT /note="Probable mannan endo-1,4-beta-mannosidase A" FT /id="PRO_5000220000" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q99036" FT ACT_SITE 314 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q99036" FT BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 205 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 281 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 344 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT CARBOHYD 17 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 194 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 71..84 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:3WH9" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 125..137 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 155..163 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 175..191 FT /evidence="ECO:0007829|PDB:3WH9" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 215..231 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 264..268 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 275..280 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 291..306 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 310..315 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 321..334 FT /evidence="ECO:0007829|PDB:3WH9" FT STRAND 338..344 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 367..372 FT /evidence="ECO:0007829|PDB:3WH9" FT HELIX 374..381 FT /evidence="ECO:0007829|PDB:3WH9" SQ SEQUENCE 383 AA; 41247 MW; 926472E9197CF491 CRC64; MKLSNALLTL ASLALANVST ALPKASPAPS TSSSAASTSF ASTSGLQFTI DGETGYFAGT NSYWIGFLTD NADVDLVMGH LKSSGLKILR VWGFNDVTSQ PSSGTVWYQL HQDGKSTINT GADGLQRLDY VVSSAEQHDI KLIINFVNYW TDYGGMSAYV SAYGGSGETD FYTSDTMQSA YQTYIKTVVE RYSNSSAVFA WELANEPRCP SCDTSVLYNW IEKTSKFIKG LDADRMVCIG DEGFGLNIDS DGSYPYQFSE GLNFTMNLGI DTIDFGTLHL YPDSWGTSDD WGNGWITAHG AACKAAGKPC LLEEYGVTSN HCSVEGSWQK TALSTTGVGA DLFWQYGDDL STGKSPDDGN TIYYGTSDYQ CLVTDHVAAI GSA //