| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G074158_T01 |
| Family | GT35 |
| Protein Properties | Length: 985 Molecular Weight: 109707 Isoelectric Point: 5.2491 |
| Chromosome | Chromosome/Scaffold: 1 Start: 278183921 End: 278192926 |
| 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 | 170 | 978 | 0 |
| ALKQLGQNLEDVASQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYEYGLFKQIITKDGQEEIAENWLEMGYPWEVVRNDVSYPVKFYGKVVEGT DGRKHWIGGENIKAVAHDVPIPGYKTRTTNNLRLWSTTVPAQDFDLAAFNSGDHTKAYEAHLNAKKICHILYPGDESLEGKVLRLKQQYTLCSASLQDII ARFESRAGESLNWEDFPSKVAVQMNDTHPTLCIPELMRILMDVKGLSWSEAWSITERTVAYTNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDEELINN IVSKYGTTDTELLKKKLKEMRILDNVDLPASISQLFVKPKDKKESPAKSKQKLLVKSLETIVDVEEKTELEEEAEVLSEIEEEKLESEEVEAEEESSEDE LDPFVKSDPKLPRVVRMANLCVVGGHSVNGVAEIHSEIVKQDVFNSFYEMWPTKFQNKTNGVTPRRWIRFCNPALSALISKWIGSDDWVLNTDKLAELKK FADNEDLHSEWRAAKKANKMKVVSLIREKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSTEERAKSFVPRVCIFGGKAFATYIQAKRI VKFITDVAATVNHDSDIGDLLKVVFVPDYNVSVAEALIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGEENFFLFGAEAHEIA GLRKERAEGKFVPDPRFEEVKEFVRSGVFGTYSYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDEAYRDQKLWTRMSILNTAGSSKFSSDRTIH EYAKDIWDI | |||
| Full Sequence |
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| Protein Sequence Length: 985 Download |
| MATTTSPPLQ LASASRPHAS ASGGGGGGGV LLAGGSGGGV APGWGRGRLQ RRVSARSVAS 60 DRDVQGPVSP AEGLPSVLNS IGSSAIASNI KHHAEFAPLF SPDHFSPLKA YHATAKSVLD 120 ALLINWNATY DYYNKMNVKQ AYYLSMEFLQ GRALTNAIGN LEITGEYAEA LKQLGQNLED 180 VASQEPDAAL GNGGLGRLAS CFLDSLATLN YPAWGYGLRY EYGLFKQIIT KDGQEEIAEN 240 WLEMGYPWEV VRNDVSYPVK FYGKVVEGTD GRKHWIGGEN IKAVAHDVPI PGYKTRTTNN 300 LRLWSTTVPA QDFDLAAFNS GDHTKAYEAH LNAKKICHIL YPGDESLEGK VLRLKQQYTL 360 CSASLQDIIA RFESRAGESL NWEDFPSKVA VQMNDTHPTL CIPELMRILM DVKGLSWSEA 420 WSITERTVAY TNHTVLPEAL EKWSLDIMQK LLPRHVEIIE TIDEELINNI VSKYGTTDTE 480 LLKKKLKEMR ILDNVDLPAS ISQLFVKPKD KKESPAKSKQ KLLVKSLETI VDVEEKTELE 540 EEAEVLSEIE EEKLESEEVE AEEESSEDEL DPFVKSDPKL PRVVRMANLC VVGGHSVNGV 600 AEIHSEIVKQ DVFNSFYEMW PTKFQNKTNG VTPRRWIRFC NPALSALISK WIGSDDWVLN 660 TDKLAELKKF ADNEDLHSEW RAAKKANKMK VVSLIREKTG YIVSPDAMFD VQVKRIHEYK 720 RQLLNILGIV YRYKKMKEMS TEERAKSFVP RVCIFGGKAF ATYIQAKRIV KFITDVAATV 780 NHDSDIGDLL KVVFVPDYNV SVAEALIPAS ELSQHISTAG MEASGTSNMK FAMNGCILIG 840 TLDGANVEIR EEVGEENFFL FGAEAHEIAG LRKERAEGKF VPDPRFEEVK EFVRSGVFGT 900 YSYDELMGSL EGNEGYGRAD YFLVGKDFPS YIECQEKVDE AYRDQKLWTR MSILNTAGSS 960 KFSSDRTIHE YAKDIWDISP AILP* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 3.0e-135 | 170 | 474 | 306 | + 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 | 581 | 978 | 403 | + 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 | 91 | 474 | 388 | + 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 | 582 | 980 | 404 | + 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 | 582 | 978 | 402 | + 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 |
| GenBank | AAK15695.1 | 0 | 56 | 984 | 1 | 928 | AF327055_1 alpha 1,4-glucan phosphorylase L isozyme [Oryza sativa] |
| GenBank | ACC59201.1 | 0 | 4 | 984 | 3 | 971 | plastid alpha-1,4-glucan phosphorylase [Triticum aestivum] |
| GenBank | ACF94692.1 | 0 | 136 | 984 | 1 | 849 | starch phosphorylase 1 precursor [Zea mays] |
| DDBJ | BAG49328.1 | 0 | 4 | 984 | 3 | 978 | plastidial starch phosphorylase 1 [Oryza sativa Japonica Group] |
| GenBank | EEC76210.1 | 0 | 4 | 984 | 3 | 964 | hypothetical protein OsI_13605 [Oryza sativa Indica Group] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2azd_B | 0 | 584 | 976 | 404 | 792 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 2azd_B | 0 | 137 | 463 | 57 | 375 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 2azd_A | 0 | 584 | 976 | 404 | 792 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 2azd_A | 0 | 137 | 463 | 57 | 375 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| PDB | 2aw3_B | 0 | 584 | 976 | 404 | 792 | A Chain A, Crystal Structure Of The Catalytic Domain Of Xylanase A From Streptomyces Halstedii Jm8 |
| Hydropathy |
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