| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr2g014460.1 |
| Family | GT35 |
| Protein Properties | Length: 1056 Molecular Weight: 119836 Isoelectric Point: 6.5515 |
| Chromosome | Chromosome/Scaffold: 2 Start: 4381210 End: 4395889 |
| Description | alpha-glucan phosphorylase 2 |
| 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 | 271 | 1048 | 0 |
| ALNQLGFEFEVLAEQEGDASLGNGGLARFSACQMDSLATLDYPAWGYGLRYEYGLFRQIIVDGFQHEQPDYWLNYGNPWEIERIHVTYEVKFYGTVEEVD MNGEKLKVWIPGETNIFYNSFSFMLTSTCVTSDLYFGTLIIWINKLVSPGKVNTNAVFGSEERSGGEIMHSVFDSQMERKVEAVAYDNPIPGYGTRNTIN LRLWAAKPSNQFDLEAYNTGDYINSIVNRQRTETISNVLYPDDRSHQGKEMRLKQQYFFVSASLQDIIRRFKEEHTNFDELPEQVALHLNDTHPSLSIAE IMRILVDEEHLEWNKAWKIVCKVFSFTTHTVVAEGLEKIPVDLLGSLLPRHLQILYEINSNFMEELKKRIGLDYNRLSRMSIVEEGAVKSIRMAILSIVC SHTVNGVSKLHANTLKTKTFKDFYELWPEKFQYTTNGVTQRRWIVVSNPSLCVLLSKWLGTEAWIRNADLLTGLRDHVDNTDFRQEWKMVKRLNKMRLAE YIETMSGVKVSLDAMFDVQVKRIHEYKRQLLNIFGIIHRYDCLKNMDKNDRRKVVPRVCIIGGKAAPGYEIAKKIIKLCHAAAEKINNDADIGDLLKLVF IPDYNVSVAELVIPGADLSQHLSTAGHEASGTGSMKFLMNGCLLLATADGSTVEIIEEIGPDNLFLFGAKVQEVAELREKGGTVKVPLQFARVLRMVRDG YFGDKDYFQSLCDTVEVDSDFYLLGSDFGSYLEAQAAADKAFVEPEKWIKMSILSAAGSGRFSSDRTIREYAERTWKI | |||
| Full Sequence |
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| Protein Sequence Length: 1056 Download |
| MQTISFPLLT NTLSFPNPLT SFPPFSIHFP TALPNNRLRV SASSPSTSST ITVENSTSDN 60 STAFLIRARN KIGLLQIITR VFKILGLTID KATVEFEGDY FTKKFFVTDS HGNKIEDDEN 120 LERIKRALTE AIGGNGDGGG KVSVSTANRG IVVRRAGLVE GFGERKAKAE RMFSLMDGFL 180 KNDPFSLQKD ILHHVEYTVA RSRFSFDDYE AYQALAHSVR DRLIERWHDT HIYFKKTKSK 240 RLYFLSLEFL MGRSLSNSVI NLGIQDQYAE ALNQLGFEFE VLAEQEGDAS LGNGGLARFS 300 ACQMDSLATL DYPAWGYGLR YEYGLFRQII VDGFQHEQPD YWLNYGNPWE IERIHVTYEV 360 KFYGTVEEVD MNGEKLKVWI PGETNIFYNS FSFMLTSTCV TSDLYFGTLI IWINKLVSPG 420 KVNTNAVFGS EERSGGEIMH SVFDSQMERK VEAVAYDNPI PGYGTRNTIN LRLWAAKPSN 480 QFDLEAYNTG DYINSIVNRQ RTETISNVLY PDDRSHQGKE MRLKQQYFFV SASLQDIIRR 540 FKEEHTNFDE LPEQVALHLN DTHPSLSIAE IMRILVDEEH LEWNKAWKIV CKVFSFTTHT 600 VVAEGLEKIP VDLLGSLLPR HLQILYEINS NFMEELKKRI GLDYNRLSRM SIVEEGAVKS 660 IRMAILSIVC SHTVNGVSKL HANTLKTKTF KDFYELWPEK FQYTTNGVTQ RRWIVVSNPS 720 LCVLLSKWLG TEAWIRNADL LTGLRDHVDN TDFRQEWKMV KRLNKMRLAE YIETMSGVKV 780 SLDAMFDVQV KRIHEYKRQL LNIFGIIHRY DCLKNMDKND RRKVVPRVCI IGGKAAPGYE 840 IAKKIIKLCH AAAEKINNDA DIGDLLKLVF IPDYNVSVAE LVIPGADLSQ HLSTAGHEAS 900 GTGSMKFLMN GCLLLATADG STVEIIEEIG PDNLFLFGAK VQEVAELREK GGTVKVPLQF 960 ARVLRMVRDG YFGDKDYFQS LCDTVEVDSD FYLLGSDFGS YLEAQAAADK AFVEPEKWIK 1020 MSILSAAGSG RFSSDRTIRE YAERTWKIDP CQCPI* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 2.0e-43 | 271 | 384 | 114 | + 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-100 | 188 | 384 | 197 | + 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 | 451 | 1048 | 604 | + 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 | 450 | 1050 | 607 | + 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 | 448 | 1048 | 607 | + 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 | CBI30609.1 | 0 | 176 | 1054 | 1 | 813 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_001694015.1 | 0 | 40 | 1054 | 57 | 997 | starch phosphorylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002273615.1 | 0 | 172 | 1054 | 1 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002305114.1 | 0 | 172 | 1054 | 1 | 817 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002509431.1 | 0 | 1 | 1054 | 1 | 948 | 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 | 412 | 1051 | 212 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1ygp_B | 0 | 187 | 458 | 44 | 318 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1ygp_A | 0 | 412 | 1051 | 212 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1ygp_A | 0 | 187 | 458 | 44 | 318 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 2ati_B | 0 | 451 | 1055 | 221 | 834 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO779924 | 684 | 82 | 762 | 0 |
| HO586252 | 541 | 513 | 1051 | 0 |
| HO802292 | 348 | 714 | 1056 | 0 |
| HO417459 | 283 | 666 | 948 | 0 |
| HO779924 | 29 | 53 | 81 | 0.019 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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