ID   MAN2_SOLLC              Reviewed;         414 AA.
AC   Q9FZ03;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase 2;
DE            EC=3.2.1.78;
DE   AltName: Full=Beta-mannanase 2;
DE   AltName: Full=Endo-beta-1,4-mannanase 2;
DE   AltName: Full=LeMAN2;
DE   Flags: Precursor;
GN   Name=MAN2;
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], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=cv. Moneymaker; TISSUE=Seed;
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).
RN   [2]
RP   SEQUENCE REVISION TO 170-174.
RA   Nonogaki H., Gee O.H., Bradford K.J.;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possesses endo-beta-mannanase activity in vitro. May be
CC       involved in seed germination by weakening the endosperm cap prior to
CC       radicle emergence. {ECO:0000269|PubMed:10938343}.
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 specifically in the endosperm cap before
CC       radicle emergence. {ECO:0000269|PubMed:10938343}.
CC   -!- INDUCTION: By gibberellin. {ECO:0000269|PubMed:10938343}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AF184238; AAG00315.2; -; mRNA.
DR   RefSeq; NP_001234473.1; NM_001247544.2.
DR   AlphaFoldDB; Q9FZ03; -.
DR   SMR; Q9FZ03; -.
DR   STRING; 4081.Solyc06g064520.2.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   PaxDb; Q9FZ03; -.
DR   PRIDE; Q9FZ03; -.
DR   GeneID; 544170; -.
DR   KEGG; sly:544170; -.
DR   eggNOG; ENOG502QTAQ; Eukaryota.
DR   HOGENOM; CLU_031603_0_0_1; -.
DR   OrthoDB; 1003648at2759; -.
DR   PhylomeDB; Q9FZ03; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q9FZ03; 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   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..414
FT                   /note="Mannan endo-1,4-beta-mannosidase 2"
FT                   /id="PRO_5000057062"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   414 AA;  46835 MW;  2ED692448896046E CRC64;
     MAYFQRLISC IFVLFLLSLA FACEARVLLD ENNANDQGFV RVNGAHFELN GSPFLFNGFN
     SYWLMHVAAE PSERYKVSEV LREASSAGLS VCRTWAFSDG GDRALQISPG VYDERVFQGL
     DFVISEAKKY GIRLILSFVN NYNDFGGKAQ YVQWARNAGA QINGDDDFYT NYITKNYYKN
     HIKKVVTRFN TITGMTYKDD STIMAWELMN EPRNQADYSG NTLNAWVQEM ASFVKSLDNK
     HLLEIGMEGF YGDSVPERKS INPGYQVGTD FISNHLIKEI DFATIHAYTD QWLSGQSDDA
     QMIFMQKWMT SHWQDAKNIL KKPLVLAEFG KSSRDPGYNQ NIRDTFMSTI YRNIYSLAKD
     GGTMGGSLIW QLVAQGMENY EDGYCIELGK NPSTAGIITS QSHAMTALAH LVKI