| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma19g03490.1 |
| Family | GT35 |
| Protein Properties | Length: 982 Molecular Weight: 110341 Isoelectric Point: 5.1341 |
| Chromosome | Chromosome/Scaffold: 19 Start: 3513140 End: 3524353 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 183 | 976 | 0 |
| ALSKLGHKLENVAYQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQRITKDGQEEVAEDWLEMGNPWEIIRNDVSYPVKFYGKVVSGS DGKKHWIGGEDIKAVAHDVPIPGYKTKTTINLRLWSTKAASEEFDLSAFNAGRHTEASEALANAEKICYILYPGDEPIEGKILRLKQQYTLCSASLQDII ARFERRSGANVNWEEFPEKVAVQMNDTHPTLCIPELMRILIDVKGLNWKDAWNITQRTVAYTNHTVLPEALEKWSLDLMQKLLPRHIEIIEMIDEELVRT IIAEYGTENSDLLEKKLKEMRILENVELTAEFADILVKSKEAIDIPSEELQSSEQAEAEDEKDDDEVEAVAKKNGTDESSIEDEKEELPEPVPEPPKLVR MANLCVVGGHAVNGVAEIHSEIVKDDVFNAFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSKIITEWIGTEDWVLNTGKLAELRKFVDNEDLQVQWREAKR SNKVKVAAFIREKTGYSVSPDAMFDIQVKRIHEYKRQLMNIFGIVYRYKKMKEMSAAEREANFVPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDPE IGDLLKVVFVPDYNVSVAEMLIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGADNFFLFGAKAHEIAGLRKERAEGKFVPDPR FEEVKEFVRSGIFGSYNYDELMGSLEGNEGFGRADYFLVGKDFPSYIECQEKVDEAYRDQTKWTRMSILNTAGSYKFSSDRTIHEYAREIWNIE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 982 Download |
| MASSSTTMRF SAASTGAAAA LPRRSSVAGF IGVAARSSAK SRLRFIGRNA NLSLRMRRMS 60 SFSVVKCVSG SEAKVQDTVA KQQEATTSLS SFTPDASSIA SSIKYHAEFT PLFSPENFDL 120 PQAFLATAQS VRDSLIINWN ATYDYYEKLN VKQAYYLSME FLQGRALLNA IGNLELTGPY 180 AEALSKLGHK LENVAYQEPD AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ 240 RITKDGQEEV AEDWLEMGNP WEIIRNDVSY PVKFYGKVVS GSDGKKHWIG GEDIKAVAHD 300 VPIPGYKTKT TINLRLWSTK AASEEFDLSA FNAGRHTEAS EALANAEKIC YILYPGDEPI 360 EGKILRLKQQ YTLCSASLQD IIARFERRSG ANVNWEEFPE KVAVQMNDTH PTLCIPELMR 420 ILIDVKGLNW KDAWNITQRT VAYTNHTVLP EALEKWSLDL MQKLLPRHIE IIEMIDEELV 480 RTIIAEYGTE NSDLLEKKLK EMRILENVEL TAEFADILVK SKEAIDIPSE ELQSSEQAEA 540 EDEKDDDEVE AVAKKNGTDE SSIEDEKEEL PEPVPEPPKL VRMANLCVVG GHAVNGVAEI 600 HSEIVKDDVF NAFYKLWPEK FQNKTNGVTP RRWIRFCNPD LSKIITEWIG TEDWVLNTGK 660 LAELRKFVDN EDLQVQWREA KRSNKVKVAA FIREKTGYSV SPDAMFDIQV KRIHEYKRQL 720 MNIFGIVYRY KKMKEMSAAE REANFVPRVC IFGGKAFATY VQAKRIVKFI TDVGATVNHD 780 PEIGDLLKVV FVPDYNVSVA EMLIPASELS QHISTAGMEA SGTSNMKFAM NGCILIGTLD 840 GANVEIREEV GADNFFLFGA KAHEIAGLRK ERAEGKFVPD PRFEEVKEFV RSGIFGSYNY 900 DELMGSLEGN EGFGRADYFL VGKDFPSYIE CQEKVDEAYR DQTKWTRMSI LNTAGSYKFS 960 SDRTIHEYAR EIWNIEPVQL P* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 2.0e-136 | 183 | 506 | 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 | 582 | 975 | 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 | 100 | 507 | 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 | 582 | 977 | 401 | + 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 | 975 | 399 | + 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 | ACJ11757.1 | 0 | 60 | 981 | 2 | 935 | alpha-1,4 glucan phosphorylase [Gossypium hirsutum] |
| Swiss-Prot | P27598 | 0 | 56 | 981 | 34 | 955 | PHSL_IPOBA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
| Swiss-Prot | P53536 | 0 | 4 | 980 | 2 | 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 | 53 | 981 | 3 | 949 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526085.1 | 0 | 12 | 981 | 2 | 977 | 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 | 150 | 973 | 57 | 792 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2azd_A | 0 | 150 | 973 | 57 | 792 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2aw3_B | 0 | 150 | 973 | 57 | 792 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2aw3_A | 0 | 150 | 973 | 57 | 792 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2av6_B | 0 | 150 | 973 | 57 | 792 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO778303 | 864 | 123 | 982 | 0 |
| HO797178 | 423 | 560 | 982 | 0 |
| HO613954 | 523 | 460 | 982 | 0 |
| HO620767 | 401 | 582 | 982 | 0 |
| HO778303 | 126 | 2 | 125 | 8e-36 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
