| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000129346 |
| Family | GT35 |
| Protein Properties | Length: 1005 Molecular Weight: 113660 Isoelectric Point: 5.0944 |
| Chromosome | Chromosome/Scaffold: 01668257 Start: 9380 End: 15218 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GT35 | 170 | 509 | 0 |
| ALSKLGHKLENVANQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQLITKDGQEEVAEDWLEMGNPWEIVRNDVSYPVKFYGKIVTGS DGKQHWIGGEDIDAVAYDVPIPGYKTKTTINLRLWSTKASSQNFDLYAFNSGEHTKASEALANAEKICYVLYPGDESMEGKTLRLKQQYTLCSASLQDIV ARFERRSGANVKWEEFPEKVAVQMNDTHPTLCIPELMRILIDLKGLDWKEAWSITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVQIIQMIDEELIQT IISEYGTADYDLLEKKLKEMRILENVDLPAKFSDLIVKPE | |||
| GT35 | 602 | 999 | 0 |
| PKLVRMANLCVVGGHAVNGVAEIHSEIVKDEVFNSFYKLWPDKFQNKTNGVTPRRWIRFCNPDLSNIITKWIGTEDWVLNTEKLAELRKFADNQDLQTQW REAKRNNKLKVVSLIKERTGYSVNPDAMFDIQVKRIHEYKRQLMNIMGIVYRYKKMKEMSASGRKSKFVPRVCMFGGKAFSTYVQAKRIVKFIADVGATI NHDPSIGDLLKVVFVPDYNVSVAEQLIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGEDNFFLFGAKAHEIAGLRKERAEGKF VPDPRFEEVKEFVKSGVFGSYNYDELIGSLEGNEGFGQADYFLVGKDFPSYIECQEKVDEAYRDQKRWTRMSILNTAGSYKFSSDRTIHEYAKDIWNI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1005 Download |
| MAASQFSATR SGAETAWHCK SQSKLIDFGS RKNKSKLLFT RTLNRTRPFS FSVKSVLDKP 60 HELKNPIIEQ DAASEFSSFV PDAASIASSI KYHAEFTPLF SPEKFELPKA FFATAQSVRD 120 ALIVNWNATN NHYEKLNAKQ AYYLSMEFLQ GRALLNAIGN LELDGAYAEA LSKLGHKLEN 180 VANQEPDAAL GNGGLGRLAS CFLDSLATLN YPAWGYGLRY KYGLFKQLIT KDGQEEVAED 240 WLEMGNPWEI VRNDVSYPVK FYGKIVTGSD GKQHWIGGED IDAVAYDVPI PGYKTKTTIN 300 LRLWSTKASS QNFDLYAFNS GEHTKASEAL ANAEKICYVL YPGDESMEGK TLRLKQQYTL 360 CSASLQDIVA RFERRSGANV KWEEFPEKVA VQMNDTHPTL CIPELMRILI DLKGLDWKEA 420 WSITQRTVAY TNHTVLPEAL EKWSLELMEK LLPRHVQIIQ MIDEELIQTI ISEYGTADYD 480 LLEKKLKEMR ILENVDLPAK FSDLIVKPEK SSTAVPSEEI EKSEEEDESA DAEKSSTAVQ 540 SEEIEESEEE DESADAEKSS TAVLSEEIEE SEEEGESADE EKVPVKKREE EKKKKVVVEP 600 PPKLVRMANL CVVGGHAVNG VAEIHSEIVK DEVFNSFYKL WPDKFQNKTN GVTPRRWIRF 660 CNPDLSNIIT KWIGTEDWVL NTEKLAELRK FADNQDLQTQ WREAKRNNKL KVVSLIKERT 720 GYSVNPDAMF DIQVKRIHEY KRQLMNIMGI VYRYKKMKEM SASGRKSKFV PRVCMFGGKA 780 FSTYVQAKRI VKFIADVGAT INHDPSIGDL LKVVFVPDYN VSVAEQLIPA SELSQHISTA 840 GMEASGTSNM KFAMNGCILI GTLDGANVEI REEVGEDNFF LFGAKAHEIA GLRKERAEGK 900 FVPDPRFEEV KEFVKSGVFG SYNYDELIGS LEGNEGFGQA DYFLVGKDFP SYIECQEKVD 960 EAYRDQKRWT RMSILNTAGS YKFSSDRTIH EYAKDIWNIN PVELH |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 6.0e-136 | 170 | 493 | 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 605 | 999 | 400 | + 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 | 87 | 494 | 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. | ||
| pfam00343 | Phosphorylase | 0 | 605 | 1001 | 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 | 605 | 999 | 400 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0004645 | phosphorylase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI22291.1 | 0 | 18 | 1004 | 18 | 981 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P04045 | 0 | 8 | 1004 | 2 | 965 | PHSL1_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-1; Flags: Precursor |
| Swiss-Prot | P53536 | 0 | 41 | 1004 | 50 | 1002 | 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 | 40 | 1004 | 3 | 948 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526085.1 | 0 | 1 | 1004 | 1 | 976 | glycogen phosphorylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2azd_B | 0 | 603 | 997 | 402 | 792 | A Chain A, Pectin Methylesterase From Carrot |
| PDB | 2azd_B | 0 | 137 | 463 | 57 | 375 | A Chain A, Pectin Methylesterase From Carrot |
| PDB | 2azd_A | 0 | 603 | 997 | 402 | 792 | A Chain A, Pectin Methylesterase From Carrot |
| PDB | 2azd_A | 0 | 137 | 463 | 57 | 375 | A Chain A, Pectin Methylesterase From Carrot |
| PDB | 2aw3_B | 0 | 603 | 997 | 402 | 792 | A Chain A, Pectin Methylesterase From Carrot |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
 | ||||
| Hit | Length | Start | End | EValue |
| HO797178 | 399 | 606 | 1004 | 0 |
| HO778303 | 399 | 606 | 1004 | 0 |
| HO778303 | 407 | 110 | 516 | 0 |
| HO620767 | 401 | 604 | 1004 | 0 |
| HO778303 | 118 | 5 | 112 | 0.000000000002 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
