| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma20g03250.2 |
| Family | GT35 |
| Protein Properties | Length: 979 Molecular Weight: 111864 Isoelectric Point: 5.0053 |
| Chromosome | Chromosome/Scaffold: 20 Start: 2943465 End: 2952383 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
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| Family | Start | End | Evalue |
| GT35 | 169 | 493 | 0 |
| ALRKLGHNLEDVANKEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQHITKDGQVEVAENWLEMGNPWEILKNDVSYPVKFYGEVISGP NGSKQWVGGENILAVAYDVPIPGYKTRTTINLRLWSTKVSPEEFDLQAYNSGDHAKAYAVMKNAEKICYVLYPGDESIDGKTLRLKQQYTLCSASLQDIF ARFERRLGKRVNWDTLPDKVVVQMNDTHPTLCIPEIIRILVDVKGLSWEKAWNITKRTVAYTNHTILPEALEKWSLTLLQDLLPRHMEIIRKIDEELINE IISEYGIDDLDLFQQRLKKMRILEN | |||
| GT35 | 562 | 973 | 0 |
| NKIELKFKVDPKLPMMVRMANLCVVGGFSVNGVAEIHSKIVKEEVFDEFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSKIITKWIGTEDWVTDLEKLAIL RKFADNEDLQLEWIEAKRRNKIRVASFLKEKTGYVVNPNAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKELSAEERKDMFVPRVCIFGGKAFATYVQAK RIVKFITDVGATINSDPEIGDLLKVVFVPDYNVSVAEMLIPGSESSQHISTAGMEASGTSNMKFAMNGCIVIGTLDGANVEIREEVGEDNFFLFGARAQE IVGLRKERVEGKFVPDPRFEEVKAYVRSGVFGPYNYEELMGSLEGNEGYGRADYFLVGKDFPSYLECQEEVDKAYHDQKRWTKMSILNTAGSFKFSSDRT IHEYARDIWRIE | |||
| Full Sequence |
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| Protein Sequence Length: 979 Download |
| MAALPFSTTC RHSNSPLHHN SKTSFIGFSQ RNNIWQLFVI TKSNSRRAIR KLCVKNVTSD 60 KKQELEEPLN EQDTFNEFVP DSASIASSIK FHAEFTSPFS PEKFELNKAF FATAESVRDS 120 LIINWNATND YYERMNVKQA YYMSMEYLQG RALLNAIGNL QLSGPYAEAL RKLGHNLEDV 180 ANKEPDAALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK YGLFKQHITK DGQVEVAENW 240 LEMGNPWEIL KNDVSYPVKF YGEVISGPNG SKQWVGGENI LAVAYDVPIP GYKTRTTINL 300 RLWSTKVSPE EFDLQAYNSG DHAKAYAVMK NAEKICYVLY PGDESIDGKT LRLKQQYTLC 360 SASLQDIFAR FERRLGKRVN WDTLPDKVVV QMNDTHPTLC IPEIIRILVD VKGLSWEKAW 420 NITKRTVAYT NHTILPEALE KWSLTLLQDL LPRHMEIIRK IDEELINEII SEYGIDDLDL 480 FQQRLKKMRI LENIELPNSV MELLSITEET PAVDPVKEID VDDTDVKATE KEDGDDDDDY 540 EVVEEEQEED NEEPSVEEDT SNKIELKFKV DPKLPMMVRM ANLCVVGGFS VNGVAEIHSK 600 IVKEEVFDEF YKLWPEKFQN KTNGVTPRRW IRFCNPDLSK IITKWIGTED WVTDLEKLAI 660 LRKFADNEDL QLEWIEAKRR NKIRVASFLK EKTGYVVNPN AMFDVQVKRI HEYKRQLLNI 720 LGIVYRYKKM KELSAEERKD MFVPRVCIFG GKAFATYVQA KRIVKFITDV GATINSDPEI 780 GDLLKVVFVP DYNVSVAEML IPGSESSQHI STAGMEASGT SNMKFAMNGC IVIGTLDGAN 840 VEIREEVGED NFFLFGARAQ EIVGLRKERV EGKFVPDPRF EEVKAYVRSG VFGPYNYEEL 900 MGSLEGNEGY GRADYFLVGK DFPSYLECQE EVDKAYHDQK RWTKMSILNT AGSFKFSSDR 960 TIHEYARDIW RIEPVELA* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 6.0e-129 | 169 | 506 | 338 | + Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 3.0e-179 | 86 | 493 | 412 | + This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 577 | 972 | 401 | + This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. | ||
| pfam00343 | Phosphorylase | 0 | 578 | 974 | 402 | + Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin. | ||
| TIGR02093 | P_ylase | 0 | 577 | 972 | 401 | + glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| Gene Ontology | |
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| GO Term | Description |
| GO:0004645 | phosphorylase activity |
| GO:0005975 | carbohydrate metabolic process |
| 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 | CBI27267.1 | 0 | 1 | 975 | 1 | 930 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P53535 | 0 | 58 | 977 | 54 | 973 | PHSL2_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-2; Flags: Precursor |
| RefSeq | XP_002274575.1 | 0 | 1 | 975 | 1 | 978 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316098.1 | 0 | 1 | 977 | 1 | 952 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512108.1 | 0 | 1 | 977 | 1 | 972 | glycogen phosphorylase, putative [Ricinus communis] |
| 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 | 1z8d_A | 0 | 578 | 974 | 440 | 830 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 1z8d_A | 0 | 110 | 519 | 53 | 459 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_B | 0 | 578 | 971 | 404 | 793 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_B | 0 | 136 | 462 | 57 | 375 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_A | 0 | 578 | 971 | 404 | 793 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| Metabolic Pathways | |||
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| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO778303 | 873 | 109 | 977 | 0 |
| HO797178 | 399 | 579 | 977 | 0 |
| HO620767 | 401 | 577 | 977 | 0 |
| HO613954 | 401 | 577 | 977 | 0 |
| HO778303 | 95 | 21 | 111 | 0.00001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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