MANA_ASPNC
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 03-AUG-2022, entry version 73.
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 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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}.
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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 PaxDb; A2QKT4; -.
DR EnsemblFungi; CAK96471; CAK96471; An05g01320.
DR GeneID; 4980871; -.
DR KEGG; ang:ANI_1_160044; -.
DR VEuPathDB; FungiDB:An05g01320; -.
DR HOGENOM; CLU_031603_4_1_1; -.
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 InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; PTHR31451; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 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
