y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10437129g0010 |
Family | GT35 |
Protein Properties | Length: 571 Molecular Weight: 65000.8 Isoelectric Point: 8.3199 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT35 | 8 | 566 | 0 |
QICAVLYPGDATEEGKLLRLKQQFFLCSASLQDIIVRFKERRHENEPIVWSEFPNKVAIQMNDTHPTLAIPELMRILMDQEGLGWDEAWAVTSRTIAYTN HTVLPEALEKWAVALIAKLLPRHMEIIVEINKRFLEMIRSSQPNMVSRLNNMRIIDDSNPLKPAVRMANLCVVSSHTVNGVALLHSNILKDELFQDYYSL WPEKFQNKTNGITPRRWLRFCSPELSAIITKWLKTSQWVTNLDLLSGLRQFADNSKLQSEWASAKMANKVRLAQYIFQVTGVEVNPNSLFDIQIKRIHEY KRQLLNILGAIYRYKKLKEMSSKERKNVVPRTVMLGGKAFATYTQAKRIVKLVNDVGAVVNNDPDIGDLLKVVFIPNYNVSVAEIIIPGSELSQHISTAG MEASGTSNMKFALNGCLIIGTLDGANVEIREEIGEDNFFLFGAQAHDVPKLRREREQGLFVPDPRFEEAKQFVKSHAFGDYDYTPLLDSLEGNTGYGRGD YFLVGYDFPSYMEAQSRVDDAYKDTKKWIKMSILSTAGSGKFSSDRTISQYAKDIWNIK |
Full Sequence |
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Protein Sequence Length: 571 Download |
MVNGEILQIC AVLYPGDATE EGKLLRLKQQ FFLCSASLQD IIVRFKERRH ENEPIVWSEF 60 PNKVAIQMND THPTLAIPEL MRILMDQEGL GWDEAWAVTS RTIAYTNHTV LPEALEKWAV 120 ALIAKLLPRH MEIIVEINKR FLEMIRSSQP NMVSRLNNMR IIDDSNPLKP AVRMANLCVV 180 SSHTVNGVAL LHSNILKDEL FQDYYSLWPE KFQNKTNGIT PRRWLRFCSP ELSAIITKWL 240 KTSQWVTNLD LLSGLRQFAD NSKLQSEWAS AKMANKVRLA QYIFQVTGVE VNPNSLFDIQ 300 IKRIHEYKRQ LLNILGAIYR YKKLKEMSSK ERKNVVPRTV MLGGKAFATY TQAKRIVKLV 360 NDVGAVVNND PDIGDLLKVV FIPNYNVSVA EIIIPGSELS QHISTAGMEA SGTSNMKFAL 420 NGCLIIGTLD GANVEIREEI GEDNFFLFGA QAHDVPKLRR EREQGLFVPD PRFEEAKQFV 480 KSHAFGDYDY TPLLDSLEGN TGYGRGDYFL VGYDFPSYME AQSRVDDAYK DTKKWIKMSI 540 LSTAGSGKFS SDRTISQYAK DIWNIKECRI P 600 |
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 | 8 | 565 | 563 | + 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 | 8 | 567 | 565 | + 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 | 8 | 565 | 563 | + 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]. | ||
PRK14985 | PRK14985 | 0 | 12 | 566 | 568 | + maltodextrin phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 9 | 566 | 562 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAM29154.1 | 0 | 8 | 569 | 281 | 838 | starch phosphorylase type H [Citrus hybrid cultivar] |
Swiss-Prot | P32811 | 0 | 8 | 571 | 276 | 838 | PHSH_SOLTU RecName: Full=Alpha-glucan phosphorylase, H isozyme; AltName: Full=Starch phosphorylase H |
RefSeq | XP_002280732.1 | 0 | 2 | 571 | 276 | 843 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313399.1 | 0 | 8 | 571 | 291 | 853 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520435.1 | 0 | 8 | 571 | 287 | 849 | 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 | 2ffr_A | 0 | 9 | 569 | 264 | 820 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 2gj4_A | 0 | 9 | 569 | 264 | 820 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3l7d_A | 0 | 9 | 569 | 276 | 832 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3l7c_A | 0 | 9 | 569 | 276 | 832 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3l7b_A | 0 | 9 | 569 | 276 | 832 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO586252 | 553 | 17 | 568 | 0 |
HO418036 | 504 | 5 | 486 | 0 |
FS996006 | 366 | 168 | 533 | 0 |
HO613954 | 498 | 122 | 571 | 0 |
HO620767 | 401 | 172 | 571 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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