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Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre12.g501900.t1.2 |
Family | GH32 |
Protein Properties | Length: 1994 Molecular Weight: 198181 Isoelectric Point: 5.4885 |
Chromosome | Chromosome/Scaffold: 12 Start: 2901361 End: 2911466 |
Description | beta-fructofuranosidase 5 |
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 | 419 | 641 | 0 |
HVMPLSGWGSDPNGPIFYKGRYHLFYQSRPGTCQWYWGMRWDHVVSSDLAHWSRLPPALCPTPGGIDADGCFSGSIQVDPHSGIPVCFYTAARLRTNRDV TLPHPPAEHDMGLKHIETQCCAICDPDDDLLVRWRKVPMPLMQLPPSGQLTAWRDPWFVEHGDGRGRQWTMLIGSGLKGGGGTALVYRSADITRGWYFAG HLCSWPDPGTGICWECPFLVQLQ |
Full Sequence |
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Protein Sequence Length: 1994 Download |
METPCTQPQQ HQQPPAGITS SANGSGGNTS HGSGSGGDAA VVTAAAALLP FRQSIPGACL 60 PPLPQCMGPV HEAPATCSTY PEHNIHAHAA PDAPAMQQLP LLAAATGGSS GGGASPAPLL 120 APPLEPPTAA ATATASPFSA VCTSSSSGSG GAAPAATAGL PAAAIAAATA ATCYGQQPAC 180 GPTSPDTEGW QEACCAALLQ RHASEGAPAL PLNAPGSPAA SDLEDFTRQI RVQHQRQHQH 240 HDSFWRLADE GSGVASEAET APTAGRHHMG AAAAVAPSTD GGHAQPPPHF MTPADFLHQK 300 HVEHHHLQQQ QQQQEQVKQR QRQRQRARRL STQQRDAAQV AAAPAGPEEE VEAEKPAAVT 360 AAPGDATTAA ALAAAGAQDS ATAAAADATA PARAGPAAAA AAASAAATAA ADSCKPLFHV 420 MPLSGWGSDP NGPIFYKGRY HLFYQSRPGT CQWYWGMRWD HVVSSDLAHW SRLPPALCPT 480 PGGIDADGCF SGSIQVDPHS GIPVCFYTAA RLRTNRDVTL PHPPAEHDMG LKHIETQCCA 540 ICDPDDDLLV RWRKVPMPLM QLPPSGQLTA WRDPWFVEHG DGRGRQWTML IGSGLKGGGG 600 TALVYRSADI TRGWYFAGHL CSWPDPGTGI CWECPFLVQL QPLPLCAHVL PTTDLAAVAG 660 AAAEATAVAE ALTTAMDYMA AMASAAGNGG GGGGSGSAAD GEGGGGGGDA AAAGTHAGSW 720 RATAQAGKVS TAAVAAATAA AEAAGDASPD AAVSVAMAAA AAAAVATVNA ATAAADAASS 780 ATQPHHAPAA GSGTAADADV DGRGACTSVR DGGSGGGDGG CDGGLVDTLL HVVTSVSAVT 840 PPTADGFAGG SEAGGGGGLP TLPSSSGIVP GGGGGGGSSA VHAVLPTADG AGIGISVTAA 900 AAPAGPDGAP GGADGSTITV TVTRAGAAAV TGPADGGGAT DDVSTAAAVG GSITTAVATV 960 TGGIEGGAPA TATIDVVVTP LASPFAAPAG GAAAAAAAAG AAGSSADGAA NGVCAPPSAP 1020 PPACPPPHPS SQRGALAPAS GRLGCAADGA PSDAAAPAAD GPLLPRQGSL TSTSVTASAK 1080 MPPASASCSG SGSGSGGVLQ DLHAMIAQVM EAHRARTAAA AAVSSCSAAA ATTAGCLPAA 1140 GAGADAKPVA AAAPAAAAPT PSAAPGAVSS KTDVNGRTGG LRGSLTPRLH AVGRNGAVAP 1200 LGTFIAGVAQ PATKSNTSNT SNSGGSPPPA SSSTCSRSSS ASSTAASSPV AGDFDGVYVL 1260 GSADDQPAAN AAAADASATA SATADADAAD GGGELLQPHQ LWYRPGMVGH CASPERAIPV 1320 EPLAADLLLQ PQPQPELQPP QLPPHPTDGA ATAATPATTL TMSYHKAQPL LPPGASYSAC 1380 VAAASALPLH GDVDSATSHA HAVALPPGRR WLFCCAPDAC TYSILYWISE YDSAAARYDM 1440 GGAEAGGRPR KLDLGNVLYA PTCLKDPQGR NVLWGYMKEL RNVPAPPCLC NKYSYAGCLS 1500 LPRALYLRGD KLFQVPLPEL TSLRSDVAVH VSALGLAPGG HWRLSGVRGL HLDMELAISP 1560 GRSRRVVVLF RSWRPRGRGA AALVYEWRTR RLFVVFEALS PAGRRKWSSG GGEGEEGHRH 1620 HHHRHAPERD QEQQEPDGLQ RELRRVQREQ QVGGAGGGGA GGGGAGGGEV AVGAPSVLAT 1680 ALPAPLVREP RGGTAAAEEG SPPPAPVPPQ QGPQEPQGEL RKDGAADGGA RESGSSSSST 1740 CSEQDHEVDG LGGAEDGDED EEEDEEENDE YDVIRDPDFI PDPDMNPLVE DWIRMKRDEA 1800 GGELDLPPGC PLRLRLFLDA SCLEVFTGTG QALTTRIYRG HPPQHCHHVP PWGSPAATSA 1860 PACAPGGPAP DPGIEIWAIG GDGDGGGAAA ATANGAGSSN GSGSSTTSGS SRHVGCTLDD 1920 VHVYEMSSGW VREQDVPREE PPPATAAAAP PAPPAPPATM APLKQQRGVR QSLSQPASPL 1980 PPSVLRGQRE RAS* 2040 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00640 | Glyco_32 | 3.0e-9 | 1408 | 1585 | 185 | + Glycosyl hydrolases family 32. | ||
cd08996 | GH32_B_Fructosidase | 2.0e-11 | 1405 | 1519 | 121 | + 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. | ||
pfam00251 | Glyco_hydro_32N | 7.0e-39 | 419 | 650 | 241 | + 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. | ||
cd08996 | GH32_B_Fructosidase | 1.0e-42 | 425 | 640 | 216 | + 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 | 2.0e-43 | 419 | 641 | 228 | + Glycosyl hydrolases family 32. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001690911.1 | 0 | 421 | 650 | 1 | 230 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001690911.1 | 0.000000000000001 | 1412 | 1508 | 620 | 707 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001690911.1 | 0.00005 | 1799 | 1840 | 920 | 963 | glycoside-hydrolase-like protein [Chlamydomonas reinhardtii] |
RefSeq | XP_001691098.1 | 0 | 399 | 649 | 3 | 254 | predicted protein [Chlamydomonas reinhardtii] |
RefSeq | YP_002753177.1 | 8e-31 | 401 | 635 | 33 | 260 | glycosyl hydrolase family, 32 [Acidobacterium capsulatum ATCC 51196] |
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 | 1uyp_F | 4e-25 | 415 | 640 | 3 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
PDB | 1uyp_E | 4e-25 | 415 | 640 | 3 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
PDB | 1uyp_D | 4e-25 | 415 | 640 | 3 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
PDB | 1uyp_C | 4e-25 | 415 | 640 | 3 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
PDB | 1uyp_B | 4e-25 | 415 | 640 | 3 | 197 | A Chain A, The Three-Dimensional Structure Of Beta-Fructosidase (Invertase) From Thermotoga Maritima |
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 | 210 | 415 | 620 | 0 |
BG844411 | 203 | 415 | 613 | 0 |
BI724909 | 166 | 415 | 578 | 7.00649e-43 |
GW237518 | 155 | 415 | 564 | 6e-40 |
BI723643 | 145 | 415 | 558 | 3e-38 |
Sequence Alignments (This image is cropped. Click for full image.) |
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