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Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre12.g488000.t1.2 |
Family | GH32 |
Protein Properties | Length: 642 Molecular Weight: 68387.2 Isoelectric Point: 4.736 |
Chromosome | Chromosome/Scaffold: 12 Start: 1414012 End: 1419219 |
Description | Glycosyl hydrolases family 32 protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH32 | 23 | 370 | 0 |
HIAPPKGWLNDPNGPLFYAGYYHMFYQHIPESCIWSFGLVWGHAVSRDLVTWEHLPPAIVPTPGGLDADGCFSGCATLDEHGVPTILYTGVRLRSNGAAG PLPPVETDLQLPFIESQCAARPVDPSDPKLTHWTKIEYPWMALPPAHWGLGGWRDPYIISRPGADGSGCWSLIIGSGVKDNGGTVLVYKSKELLDGWQLH GELCHGRGEGSTTGFIWECPLLTKLPALPAHIARGGVVSHGNASRASTSESGDDMADTPHFFCISPDACTNPSYYWLGRYDTESMTFNLKGADGPFRLDL GDILYAPNTLEDTANGRTLLWGWNQEKRTKVGAYDYAGCLSVPRILWA |
Full Sequence |
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Protein Sequence Length: 642 Download |
MTAGSQSVAK ARPAIKQDRP SFHIAPPKGW LNDPNGPLFY AGYYHMFYQH IPESCIWSFG 60 LVWGHAVSRD LVTWEHLPPA IVPTPGGLDA DGCFSGCATL DEHGVPTILY TGVRLRSNGA 120 AGPLPPVETD LQLPFIESQC AARPVDPSDP KLTHWTKIEY PWMALPPAHW GLGGWRDPYI 180 ISRPGADGSG CWSLIIGSGV KDNGGTVLVY KSKELLDGWQ LHGELCHGRG EGSTTGFIWE 240 CPLLTKLPAL PAHIARGGVV SHGNASRAST SESGDDMADT PHFFCISPDA CTNPSYYWLG 300 RYDTESMTFN LKGADGPFRL DLGDILYAPN TLEDTANGRT LLWGWNQEKR TKVGAYDYAG 360 CLSVPRILWA EPSTVAAEPS SSSSNQSSAE PSRWALHQQP VPELSRLRKT DAASCWRLSD 420 DLPGESAELI ILGSARLPLP VVSGPFLDIE LVLERADSGC TASGLLLTST TAEGGAALLY 480 HWDSGVLEVV FEALDPHTLT FSLAAPGARR VGGPLLRPPA PGQPLSLRVF LDYSCLEVFT 540 GDGEVLTARV YRGVPSSMDA AGGLAGIGAP SAAGIDIISV KDGNSDGNAG ATRILHCEAY 600 EMSPAFRLFL GAIDDEEEAL AAEPIQLPAF GAPVAVTVEA L* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 3.0e-56 | 8 | 551 | 557 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 9.0e-60 | 17 | 565 | 561 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 3.0e-74 | 29 | 369 | 346 | + Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
smart00640 | Glyco_32 | 3.0e-80 | 23 | 543 | 527 | + Glycosyl hydrolases family 32. | ||
pfam00251 | Glyco_hydro_32N | 2.0e-81 | 23 | 369 | 355 | + Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAL92880.1 | 0 | 3 | 551 | 109 | 624 | fructosyltransferase [Lolium perenne] |
RefSeq | XP_001690911.1 | 0 | 26 | 252 | 2 | 225 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001690911.1 | 9e-25 | 283 | 453 | 620 | 805 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001690911.1 | 2e-40 | 473 | 554 | 883 | 964 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001691098.1 | 0 | 1 | 292 | 1 | 292 | predicted protein [Chlamydomonas reinhardtii] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2ac1_A | 0 | 13 | 551 | 2 | 504 | A Chain A, Crystal Structure Of A Cell-Wall Invertase From Arabidopsis Thaliana |
PDB | 2xqr_K | 0 | 19 | 551 | 5 | 500 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_I | 0 | 19 | 551 | 5 | 500 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_G | 0 | 19 | 551 | 5 | 500 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_E | 0 | 19 | 551 | 5 | 500 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
fructan biosynthesis | RXN-1781 | EC-2.4.1.99 | sucrose:sucrose fructosyltransferase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BI723642 | 211 | 15 | 225 | 0 |
BG844411 | 205 | 14 | 218 | 0 |
BM003195 | 217 | 231 | 447 | 0 |
BI724909 | 168 | 15 | 182 | 0 |
BI718454 | 197 | 233 | 429 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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