MAN4_SOLLC
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 03-AUG-2022, entry version 98.
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}.
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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.Solyc01g008710.2.1; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; Q8L5J1; -.
DR PRIDE; Q8L5J1; -.
DR GeneID; 543823; -.
DR KEGG; sly:543823; -.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_0_0_1; -.
DR InParanoid; Q8L5J1; -.
DR OrthoDB; 1003648at2759; -.
DR PhylomeDB; Q8L5J1; -.
DR BRENDA; 3.2.1.78; 3101.
DR EvolutionaryTrace; Q8L5J1; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q8L5J1; 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 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
