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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 148158 |
Family | GT35 |
Protein Properties | Length: 819 Molecular Weight: 94197.6 Isoelectric Point: 6.3607 |
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 | 100 | 813 | 0 |
ALKQLGFDLEILVEQERDAALGNGGLGRLAACFLDSLATLDYPAWGYGLRYEYGMFRQTIQDGFQLEHPDYWLNFGNPWEIQRVHTTYPVKFYGHVDEIQ ENNKKTYIWTPGETVEAVAYDNPIPGYGTKNTINLRLWAAKPSGELELDSFSTGDYVNAVLSKQRAETISSILYPDDRTYQGKELRLKQQVFLVSASLQD VVRRYKDFHSDFAAFPQKVAFQLNDTHPIIGVAELMRILLDEEKLDWVKSWEITTKVFSFTNHAILPEALEKWPLELLENLLPRHLQIIYRINFYFMEEM KKKFGDDLVRLSRLSIIEEGEKKNVRMANLALVSCHTVNGVSKSHFEFIKSSLFKDFHDMWPHKFQCKTNGVTQRRWMACSNPDLSQLITKWLGTEAWLK ELDLLLGLRLHANDYNLQEQWMKVRRSNKSRLAAYIQIISGAKVNVDAMFDVQIKRIHEYKRQFLNVIGIIHRYDCIKNMTAEDRKKVVPRVCILGGKAP PGYENAKRIIKLIHAVGDKLNNDPDVGDLLKLIFIPDYNVSMAELVIPASDISQHLSTAGSEACGTGNMKFAMNGCLIVGTKDGSNVEIQEELGSENMFL FGPSAEDIPELRTEQKDFQPVLEFRRVVGMIRKGVFGNAEYFQPLCDTIDGAGDDYYLLGHDFPSYLEAQAAVDKAFVDKKRWAEMSILSTAGCGQFSTD RTIREYAEEIWNVE |
Full Sequence |
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Protein Sequence Length: 819 Download |
MYKLMDQYLK NDTFSIQKNI VDHSEYTLAR SRFRFDDFEA YQATAYSVRD RLIERWNDTH 60 SLMREKDPKR IYYLSMEFLM GRSLLNSIVN IGVKGQYADA LKQLGFDLEI LVEQERDAAL 120 GNGGLGRLAA CFLDSLATLD YPAWGYGLRY EYGMFRQTIQ DGFQLEHPDY WLNFGNPWEI 180 QRVHTTYPVK FYGHVDEIQE NNKKTYIWTP GETVEAVAYD NPIPGYGTKN TINLRLWAAK 240 PSGELELDSF STGDYVNAVL SKQRAETISS ILYPDDRTYQ GKELRLKQQV FLVSASLQDV 300 VRRYKDFHSD FAAFPQKVAF QLNDTHPIIG VAELMRILLD EEKLDWVKSW EITTKVFSFT 360 NHAILPEALE KWPLELLENL LPRHLQIIYR INFYFMEEMK KKFGDDLVRL SRLSIIEEGE 420 KKNVRMANLA LVSCHTVNGV SKSHFEFIKS SLFKDFHDMW PHKFQCKTNG VTQRRWMACS 480 NPDLSQLITK WLGTEAWLKE LDLLLGLRLH ANDYNLQEQW MKVRRSNKSR LAAYIQIISG 540 AKVNVDAMFD VQIKRIHEYK RQFLNVIGII HRYDCIKNMT AEDRKKVVPR VCILGGKAPP 600 GYENAKRIIK LIHAVGDKLN NDPDVGDLLK LIFIPDYNVS MAELVIPASD ISQHLSTAGS 660 EACGTGNMKF AMNGCLIVGT KDGSNVEIQE ELGSENMFLF GPSAEDIPEL RTEQKDFQPV 720 LEFRRVVGMI RKGVFGNAEY FQPLCDTIDG AGDDYYLLGH DFPSYLEAQA AVDKAFVDKK 780 RWAEMSILST AGCGQFSTDR TIREYAEEIW NVEPLRHS* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 17 | 812 | 802 | + 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. | ||
TIGR02093 | P_ylase | 0 | 20 | 812 | 799 | + 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]. | ||
pfam00343 | Phosphorylase | 0 | 100 | 814 | 721 | + 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. | ||
PRK14986 | PRK14986 | 0 | 43 | 816 | 782 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 15 | 814 | 812 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
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 | 11 | 815 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 11 | 815 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 3t3i_A | 0 | 16 | 817 | 27 | 832 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 3t3h_A | 0 | 16 | 817 | 27 | 832 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 3t3g_A | 0 | 16 | 817 | 27 | 832 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
Sequence Alignments (This image is cropped. Click for full image.) |
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