Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G099400.2 |
Family | GH32 |
Protein Properties | Length: 531 Molecular Weight: 60140 Isoelectric Point: 5.885 |
Chromosome | Chromosome/Scaffold: 10 Start: 17556774 End: 17559376 |
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 | 52 | 367 | 0 |
HFQPPKNWMNDPNGPMYYKGVYHLFYQYNPYAAVWGNITWAHSISYDLVNWINLDIALSPGDPFDINGCWSGSTTFLSGEKPVILYTGSDTMNRQVQNLA EPKNLSDPLLREWVKSSHNPLMSPVDGIDPKNFRDPTTAWQGPDGLWRVLVGNEMDGHGRALLYRSQDFITWSQSKEPIHSSTRTGMWECPDFYPVSIDG KNGVETSSLDKFTKQVLKASFDNSDHYVLGNYTAVTDNFLVDTDFLDNGSDLRYDYGNFYASKTFFDSGKKRRILWGWILESDNTTDDVKKGWSGLQSIP RTILLSKTGKQLIQWP |
Full Sequence |
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Protein Sequence Length: 531 Download |
MTYLKLEVTM EKSVVLVIGF WLLLLGNGVQ SHRQDKKHQS LPRDQPYRTG YHFQPPKNWM 60 NDPNGPMYYK GVYHLFYQYN PYAAVWGNIT WAHSISYDLV NWINLDIALS PGDPFDINGC 120 WSGSTTFLSG EKPVILYTGS DTMNRQVQNL AEPKNLSDPL LREWVKSSHN PLMSPVDGID 180 PKNFRDPTTA WQGPDGLWRV LVGNEMDGHG RALLYRSQDF ITWSQSKEPI HSSTRTGMWE 240 CPDFYPVSID GKNGVETSSL DKFTKQVLKA SFDNSDHYVL GNYTAVTDNF LVDTDFLDNG 300 SDLRYDYGNF YASKTFFDSG KKRRILWGWI LESDNTTDDV KKGWSGLQSI PRTILLSKTG 360 KQLIQWPLEE IEKQRIIKVS FENKELKGGS VLEVSGITAS QADVEVSFSL SSFKEAELMD 420 PSWVDPKLLC SQKTASVRSN VGPFGILVLA SKDLTEQTAI FFRVFRSKDN YVVLMCSDQS 480 RSSVEEGPQK TIYGAFIDID PLNEKISLRS LVCYICFNTS IITFAKFSID * 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01322 | scrB_fam | 2.0e-52 | 36 | 375 | 358 | + sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
COG1621 | SacC | 3.0e-73 | 35 | 394 | 372 | + Beta-fructosidases (levanase/invertase) [Carbohydrate transport and metabolism] | ||
cd08996 | GH32_B_Fructosidase | 2.0e-94 | 58 | 370 | 327 | + 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 | 8.0e-143 | 52 | 367 | 326 | + 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. | ||
smart00640 | Glyco_32 | 3.0e-165 | 52 | 512 | 473 | + 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 |
EMBL | CAD19323.1 | 0 | 9 | 512 | 3 | 508 | exocellular acid invertase 2 [Beta vulgaris] |
RefSeq | XP_002278898.1 | 0 | 60 | 512 | 1 | 452 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002278918.1 | 0 | 10 | 512 | 1 | 502 | PREDICTED: hypothetical protein isoform 3 [Vitis vinifera] |
RefSeq | XP_002279133.1 | 0 | 64 | 512 | 2 | 448 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002309496.1 | 0 | 10 | 512 | 1 | 502 | predicted protein [Populus trichocarpa] |
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 | 2xqr_K | 0 | 44 | 512 | 1 | 479 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_I | 0 | 44 | 512 | 1 | 479 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_G | 0 | 44 | 512 | 1 | 479 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_E | 0 | 44 | 512 | 1 | 479 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 2xqr_C | 0 | 44 | 512 | 1 | 479 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CO095726 | 271 | 94 | 364 | 0 |
CT842376 | 475 | 48 | 512 | 0 |
DY273985 | 326 | 67 | 388 | 0 |
FC881182 | 304 | 67 | 366 | 0 |
JG637105 | 267 | 44 | 307 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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