Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000259799 |
Family | GT35 |
Protein Properties | Length: 695 Molecular Weight: 78398.4 Isoelectric Point: 4.7073 |
Chromosome | Chromosome/Scaffold: 013193480 Start: 11316 End: 16337 |
Description | Glycosyl transferase, family 35 |
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 |
GT35 | 175 | 515 | 0 |
ALSKLGHKLENVANQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQLITKDGQEEVAEDWLEMGNPWEIVRNDVSYPVKFYGKIVTGS DGKQHWIGGEDIDAVAYDVPIPGYKTKTTINLRLWSTKASSQNFDLYAFNSGEHTKASEALANAEKICYVLYPGDESMEGKTLRLKQQYTLCSASLQDIV ARFERRSGANVKWEEFPEKVAVQMNDTHPTLCIPELMRILIDLKGLDWKEAWSITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVQIIQMIDEELIQT IISEYGTADYDLLEKKLKEMRILENVDLPAKFSDLIVKPEK |
Full Sequence |
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Protein Sequence Length: 695 Download |
MQILHSAGSQ TVKELTHRNQ QIKACRVDVR SSASATTETM QILHSAGSQT VKELTHRNQQ 60 IKTCCVDVHF AFFYLDAASE FSSFVPDAAS IASSIKYHAE FTPLFSPEKF ELPKAFFATA 120 QSVRDALIVN WNATNNHYEK LNAKQAYYLS MEFLQGRALL NAIGNLELDG AYAEALSKLG 180 HKLENVANQE PDAALGNGGL GRLASCFLDS LATLNYPAWG YGLRYKYGLF KQLITKDGQE 240 EVAEDWLEMG NPWEIVRNDV SYPVKFYGKI VTGSDGKQHW IGGEDIDAVA YDVPIPGYKT 300 KTTINLRLWS TKASSQNFDL YAFNSGEHTK ASEALANAEK ICYVLYPGDE SMEGKTLRLK 360 QQYTLCSASL QDIVARFERR SGANVKWEEF PEKVAVQMND THPTLCIPEL MRILIDLKGL 420 DWKEAWSITQ RTVAYTNHTV LPEALEKWSL ELMEKLLPRH VQIIQMIDEE LIQTIISEYG 480 TADYDLLEKK LKEMRILENV DLPAKFSDLI VKPEKSSTAV PSEEIEKSEE EDESADAEKS 540 STAVQSEEIE ESEEEDESAD AEKSSTAVLS EEIEESEEEG ESADEEKVPV KKREEEKKKK 600 VVVEPPPKLV RMANLCVVGG HAVNGVAEIH SEIVKDEVFN SFYKLWPDKF QNKTNGVTPR 660 RWIRFCNPDL SNIITKWIGT EDWVLNTEKL AELRK |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02093 | P_ylase | 6.0e-40 | 610 | 695 | 86 | + 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]. | ||
cd04300 | GT1_Glycogen_Phosphorylase | 8.0e-44 | 610 | 695 | 86 | + 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 | 6.0e-140 | 175 | 498 | 324 | + 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 | 3.0e-174 | 95 | 499 | 408 | + 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]. | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 92 | 499 | 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. |
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 |
PRF/SEQDB | 0 | 87 | 695 | 68 | 640 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
Swiss-Prot | P27598 | 0 | 87 | 695 | 68 | 640 | PHSL_IPOBA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
Swiss-Prot | P53536 | 0 | 76 | 695 | 82 | 688 | PHSL_VICFA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
RefSeq | XP_002305367.1 | 0 | 86 | 695 | 47 | 634 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526085.1 | 0 | 77 | 695 | 75 | 662 | 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 | 1ygp_B | 0 | 115 | 489 | 68 | 455 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_B | 6e-19 | 606 | 695 | 464 | 556 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 115 | 489 | 68 | 455 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 6e-19 | 606 | 695 | 464 | 556 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1z8d_A | 0 | 85 | 498 | 22 | 433 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778303 | 407 | 115 | 521 | 0 |
ES816557 | 331 | 187 | 517 | 0 |
CO100137 | 297 | 206 | 502 | 0 |
HO778303 | 85 | 611 | 695 | 2.00386e-43 |
HO778303 | 42 | 76 | 117 | 0.000000004 |
Sequence Alignments (This image is cropped. Click for full image.) |
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