ID MAN4_SOLLC Reviewed; 399 AA. AC Q8L5J1; Q8RVL3; Q93WT4; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 27-MAR-2024, entry version 104. DE RecName: Full=Mannan endo-1,4-beta-mannosidase 4; DE EC=3.2.1.78; DE AltName: Full=Beta-mannanase 4; DE AltName: Full=Endo-beta-1,4-mannanase 4; DE AltName: Full=LeMAN4a; DE AltName: Full=LeMAN4i; DE Flags: Precursor; GN Name=MAN4; 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], PROTEIN SEQUENCE OF 27-39, FUNCTION, RP CHARACTERIZATION OF VARIANT 394-ARG--SER-399 DELINS ALA-LEU, AND RP MUTAGENESIS OF 394-ARG--SER-399. RC STRAIN=cv. Trust, and cv. Walter; TISSUE=Pericarp; RX PubMed=12427992; DOI=10.1104/pp.011890; RA Bourgault R., Bewley J.D.; RT "Variation in its C-terminal amino acids determines whether endo-beta- RT mannanase is active or inactive in ripening tomato fruits of different RT cultivars."; RL Plant Physiol. 130:1254-1262(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=cv. Castalia; TISSUE=Pericarp; RA Carrington C.M.S., Vendrell M., Dominguez-Puigjaner E.; RT "Characterisation of an endo-(1,4)-beta-mannanase expressed in ripening RT tomato fruit."; RL Plant Sci. 163:599-606(2002). RN [3] RP PROTEIN SEQUENCE OF 27-56, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16649044; DOI=10.1007/s00425-006-0286-0; RA Schroeder R., Wegrzyn T.F., Sharma N.N., Atkinson R.G.; RT "LeMAN4 endo-beta-mannanase from ripe tomato fruit can act as a mannan RT transglycosylase or hydrolase."; RL Planta 224:1091-1102(2006). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 27-399, AND DISULFIDE BOND. RX PubMed=15840830; DOI=10.1110/ps.041260905; RA Bourgault R., Oakley A.J., Bewley J.D., Wilce M.C.J.; RT "Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from RT tomato fruit."; RL Protein Sci. 14:1233-1241(2005). CC -!- FUNCTION: Possesses endo-beta-mannanase and mannan transglycosylase CC activities. May be involved in cell wall degradation during fruit CC ripening. {ECO:0000269|PubMed:12427992, ECO:0000269|PubMed:16649044}. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.0 for both endo-beta-mannanase and mannan CC transglycosylase activities. {ECO:0000269|PubMed:16649044}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in flowers and fruit pericarp. CC {ECO:0000269|Ref.2}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {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; AY046588; AAK97760.1; -; mRNA. DR EMBL; AY046589; AAK97759.2; -; mRNA. DR EMBL; AY034075; AAK56557.1; -; mRNA. DR RefSeq; NP_001234131.1; NM_001247202.2. DR PDB; 1RH9; X-ray; 1.50 A; A=27-399. DR PDBsum; 1RH9; -. DR AlphaFoldDB; Q8L5J1; -. DR SMR; Q8L5J1; -. DR STRING; 4081.Q8L5J1; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR PaxDb; 4081-Solyc01g008710-2-1; -. DR GeneID; 543823; -. DR KEGG; sly:543823; -. DR eggNOG; ENOG502QS4Q; Eukaryota. DR HOGENOM; CLU_031603_0_0_1; -. DR InParanoid; Q8L5J1; -. DR OrthoDB; 2717493at2759; -. DR PhylomeDB; Q8L5J1; -. DR BRENDA; 3.2.1.78; 3101. DR EvolutionaryTrace; Q8L5J1; -. DR Proteomes; UP000004994; Unplaced. DR ExpressionAtlas; Q8L5J1; 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:0008152; P:metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR045053; MAN-like. DR PANTHER; PTHR31451:SF39; MANNAN ENDO-1,4-BETA-MANNOSIDASE 1; 1. DR PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase; KW Hydrolase; Reference proteome; Secreted; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000269|PubMed:12427992, FT ECO:0000269|PubMed:16649044" FT CHAIN 27..399 FT /note="Mannan endo-1,4-beta-mannosidase 4" FT /id="PRO_0000277492" FT ACT_SITE 204 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q99036" FT ACT_SITE 318 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q99036" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 203 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 279 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:B4XC07" FT DISULFID 347..354 FT /evidence="ECO:0000269|PubMed:15840830" FT VARIANT 394..399 FT /note="RLSKLS -> AL (in strain: cv. Castalia and cv. FT Walter; in allele LeMAN4i; inactive enzyme)" FT /evidence="ECO:0000269|PubMed:12427992" FT MUTAGEN 394..399 FT /note="RLSKLS->ALS: Activity reduced by 5-fold." FT /evidence="ECO:0000269|PubMed:12427992" FT MUTAGEN 394 FT /note="R->A: Activity slightly reduced." FT MUTAGEN 396..399 FT /note="Missing: Activity reduced by 8-fold." FT MUTAGEN 397..399 FT /note="Missing: Activity reduced by 3-fold." FT MUTAGEN 398..399 FT /note="Missing: Activity reduced by 5-fold." FT MUTAGEN 399 FT /note="Missing: No effect on activity." FT CONFLICT 274 FT /note="T -> A (in Ref. 2; AAK56557)" FT /evidence="ECO:0000305" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:1RH9" FT TURN 64..67 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 107..122 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 133..140 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 141..150 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 158..162 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 165..180 FT /evidence="ECO:0007829|PDB:1RH9" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 214..230 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 246..251 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 262..266 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 289..310 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 330..349 FT /evidence="ECO:0007829|PDB:1RH9" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:1RH9" FT HELIX 382..395 FT /evidence="ECO:0007829|PDB:1RH9" SQ SEQUENCE 399 AA; 45339 MW; 805A7D7866E5FF6B CRC64; MNNSIILIFV AILIIFPNEF SKPTRAFSNN NFVYTDGTHF ALNGKSLYIN GFNAYWLMYI AYDPSTRIKV TNTFQQASKY KMNVARTWAF SHGGSRPLQS APGVYNEQMF QGLDFVISEA KKYGIHLIMS LVNNWDAFGG KKQYVEWAVQ RGQKLTSDDD FFTNPMVKGF YKNNVKVVLT RVNTITKVAY KDDPTILSWE LINEPRCPSD LSGKTFQNWV LEMAGYLKSI DSNHLLEIGL EGFYGNDMRQ YNPNSYIFGT NFISNNQVQG IDFTTIHMYP NQWLPGLTQE AQDKWASQWI QVHIDDSKML KKPLLIAEFG KSTKTPGYTV AKRDNYFEKI YGTIFNCAKS GGPCGGGLFW QVLGQGMSSF DDGYQVVLQE SPSTSRVILL QSLRLSKLS //