ID   MAN1_SOLLC              Reviewed;         397 AA.
AC   O48540;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 1;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 1;
DE   AltName: Full=Endo-beta-1,4-mannanase 1;
DE   AltName: Full=LeMAN1;
DE   Flags: Precursor;
GN   Name=MAN1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-88.
RC   TISSUE=Seed;
RX   PubMed=9421930; DOI=10.1007/s004250050214;
RA   Bewley J.D., Burton R.A., Morohashi Y., Fincher G.B.;
RT   "Molecular cloning of a cDNA encoding a (1-->4)-beta-mannan endohydrolase
RT   from the seeds of germinated tomato (Lycopersicon esculentum).";
RL   Planta 203:454-459(1997).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10938809; DOI=10.1093/jexbot/51.344.529;
RA   Bewley J.D., Banik M., Bourgault R., Feurtado J.A., Toorop P.,
RA   Hilhorst H.W.M.;
RT   "Endo-beta-mannanase activity increases in the skin and outer pericarp of
RT   tomato fruits during ripening.";
RL   J. Exp. Bot. 51:529-538(2000).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10938343; DOI=10.1104/pp.123.4.1235;
RA   Nonogaki H., Gee O.H., Bradford K.J.;
RT   "A germination-specific endo-beta-mannanase gene is expressed exclusively
RT   in the micropylar endosperm cap of tomato seeds.";
RL   Plant Physiol. 123:1235-1246(2000).
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   -!- DEVELOPMENTAL STAGE: Expressed in lateral endosperm after radicle
CC       emergence (72 hours germinated seeds). Expressed in fruit pericarp
CC       during the early stages of ripening. {ECO:0000269|PubMed:10938343,
CC       ECO:0000269|PubMed:10938809}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AF017144; AAB87859.2; -; mRNA.
DR   PIR; T04323; T04323.
DR   RefSeq; NP_001234575.1; NM_001247646.1.
DR   AlphaFoldDB; O48540; -.
DR   SMR; O48540; -.
DR   STRING; 4081.O48540; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; 4081-Solyc00g231680-1-1; -.
DR   EnsemblPlants; Solyc00g231680.2.1; Solyc00g231680.2.1; Solyc00g231680.2.
DR   GeneID; 544199; -.
DR   Gramene; Solyc00g231680.2.1; Solyc00g231680.2.1; Solyc00g231680.2.
DR   KEGG; sly:544199; -.
DR   eggNOG; ENOG502QTAQ; Eukaryota.
DR   InParanoid; O48540; -.
DR   OrthoDB; 2717493at2759; -.
DR   Proteomes; UP000004994; Unassembled WGS sequence.
DR   ExpressionAtlas; O48540; baseline and differential.
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   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:SF55; MANNAN ENDO-1,4-BETA-MANNOSIDASE 1; 1.
DR   PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:9421930"
FT   CHAIN           24..397
FT                   /note="Mannan endo-1,4-beta-mannosidase 1"
FT                   /id="PRO_0000277491"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   397 AA;  44804 MW;  48FD322D2B5ED37F CRC64;
     MSYARRSCIC GLFLLFLALV CEANSGFIGV KDSHFELNGS PFLFNGFNSY WLMHVAADPT
     ERYKVTEVLK DASVAGLSVC RTWAFSDGGD RALQISPGIY DERVFQGLDF VIAEAKKYGI
     RLILSFVNQW NDFGGKAQYV WWARNAGAQI SNDDEFYTHP MLKKYLKNHI EKVVTRLNSI
     TKVAYKDDPT IMAWELMNEP RDQADYSGKT VNGWVQEMAS FVKSLDNKHL LEVGMEGFYG
     DSIPERKSVN PGYQVGTDFI SNHLINEIDF ATIHAYTDQW VSGQSDDAQL VWMEKWITSH
     WEDARNILKK PLVLAEFGKS SRGQGSRDIF MSSVYRNVYN LAKEGGTMAG SLVWQLMAHG
     MENYDDGYCI VLGQTPSTTQ IISDQAHVMT ALARSLN
//