ID   MANP_ARATH              Reviewed;         408 AA.
AC   Q9LW44; F4J6N6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 3.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative mannan endo-1,4-beta-mannosidase P;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase P;
DE   AltName: Full=Endo-beta-1,4-mannanase P;
DE            Short=AtMANP;
DE   Flags: Precursor;
GN   Name=MANP; OrderedLocusNames=At3g30540; ORFNames=MQP15.18;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=16897088; DOI=10.1007/s10142-006-0034-3;
RA   Yuan J.S., Yang X., Lai J., Lin H., Cheng Z.-M., Nonogaki H., Chen F.;
RT   "The endo-beta-mannanase gene families in Arabidopsis, rice, and poplar.";
RL   Funct. Integr. Genomics 7:1-16(2007).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE77650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AEE77650.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AEE77650.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB01021.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB01021.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB01021.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB016878; BAB01021.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77650.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_189675.2; NM_113955.2.
DR   AlphaFoldDB; Q9LW44; -.
DR   SMR; Q9LW44; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PRIDE; Q9LW44; -.
DR   GeneID; 822768; -.
DR   KEGG; ath:AT3G30540; -.
DR   Araport; AT3G30540; -.
DR   InParanoid; Q9LW44; -.
DR   OrthoDB; 653343at2759; -.
DR   PhylomeDB; Q9LW44; -.
DR   BioCyc; ARA:AT3G30540-MON; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LW44; baseline.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
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   5: Uncertain;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..408
FT                   /note="Putative mannan endo-1,4-beta-mannosidase P"
FT                   /id="PRO_0000277481"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  45356 MW;  5536B88BF62A373A CRC64;
     MKCLCFIVLL AIVIAQSYVG VEAAPSDGFV SRNGVQFILN GKPFYANGFN AYWLAYEATD
     PATRFKITNV FQNATSLGLT IARTWGFRNG AIYRALQTAP GSYDEQTFQG LDFGIAEAKR
     VGIKLIIPLV NNWDDYGGKK QYVDWARSKG EMVSSNDDFY RNPVIKEFYK NHVKTMLNRV
     NTFTKVAYKD EPASMAWQLM NEPRCGVDRS GKTLMAWINE MALFVKSVDP NHLLSTGHEG
     FYGDSSPERK NSLNPVSANT VGADFIANHN IDAIDFASMH CGSDLWFQRL DQNSRLAFIK
     RWLEGHIEDA QNNLKKPVIL AEFGLGSDTP RYTLANRDDV FTTTYDIIYI STQKGGSAAG
     ALFWEVISEG VSNFAGPSSI ILSDKSSTVN IISEQRRKMG LLGGTKGK