MANA2_ASPTN
ID MANA2_ASPTN Reviewed; 396 AA.
AC Q0CUG5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable mannan endo-1,4-beta-mannosidase A-2;
DE EC=3.2.1.78;
DE AltName: Full=Endo-beta-1,4-mannanase A-2;
DE Flags: Precursor;
GN Name=manA-2; Synonyms=man1-2; ORFNames=ATEG_02669;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=EAU37631.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; CH476596; EAU37631.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001211847.1; XM_001211847.1.
DR AlphaFoldDB; Q0CUG5; -.
DR SMR; Q0CUG5; -.
DR STRING; 341663.Q0CUG5; -.
DR EnsemblFungi; EAU37631; EAU37631; ATEG_02669.
DR GeneID; 4317245; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR OMA; TQWITDH; -.
DR OrthoDB; 1003648at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..396
FT /note="Probable mannan endo-1,4-beta-mannosidase A-2"
FT /id="PRO_0000393704"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99036"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 43756 MW; D326B27A4DADC65C CRC64;
MKVPRLLLAL GGLASIHIAS ALPQGAVERD MHATSAVVHG GNVKTKFPST TGLKFTIDGE
TGYFAGSNSY WIGFLTNNAD VDLVFQHMKE SGLKILRVWG FNDVNTKPAT GTVWYQLHAN
GTSTINTGPD GLQRLDYVVH SAERHGIKLI INFVNNWNDY GGINSYLQAY GGASNEDFYN
SEPMQKAYRA YIKEVVSRYI DSPAVFAWEL ANEPRCKGCD TSVLHSWIEK TSRYIKSLDK
KHMVTTGEEG FGLDLMSDGS YPFTYVEGGN FTDTLSIPTI DFGTFHLYPS SWGTTNDWGN
LWVEAHGAAC KAAGKPRLFE EYGVTADHCA LEKPWQTTAL KTKGVSGDLY WQYGDTLSTG
PSPDDGNTFY YGTDEFDCLV SDHVAAIDEM EKHGRH