| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20001423m |
| Family | GT35 |
| Protein Properties | Length: 872 Molecular Weight: 98705.6 Isoelectric Point: 7.3487 |
| Chromosome | Chromosome/Scaffold: 23 Start: 1973514 End: 1982241 |
| Description | alpha-glucan phosphorylase 2 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 139 | 864 | 0 |
| ALNQMGYEMERVADAERDAALGNGGLGRLAACFLDSMATLDLPGWGYGIRYKYGMFKQALKNGYQVELPDIWLTKGNPWELRRDDVKYEVGFGGRVERRK QGSKEVTVWTPSERVIAQAYDNPIPGYNTPTTSNLRLWDAVPVTEFDLGAFNAGDYDRAMLERERAEGISAVLYPNDSTPEGKELRLKQQYFFVCASLQD VLSRFKAVHATDFNLLPEKACFQLNDTHPTIAVAELMRLLVDVEGLDWDQAWTITTKCLNYTNHTVMPEALEKWPVKVMAKMLPRHMEIIEVINEGWTKW LAGHLKDLKPEERAKRVAAMSIIHENPWNKDEMLVNMAYLAVVGSSAVNGVAAIHSNIVKDEILNDFYQIFPSKFQNKTNGVTPRRWLAWCNPELAALIT DALGTSEWINDTEKLAGLRAFASDKSFQAKWSAVKKAKKAKLAQLIKKVHGDDVNQEALFDIQIKRIHEYKRQYLNVLSIIWRYKQLKKMSPEERKKAVP RVCVIGGKAASAYDMAKRIIRLVTAVGDVINKDPDTQDYLRLYFLPDYNVSLAETIIPAAELSQHISTAGTEASGTSNMKFQMNGCLIIGTWDGANIEIA EETGIENVFVFGVRAEEINQLRKERKNLKTDPRWDELMRDIESGMFGDKDYFKPLVDSVNNMKVGNDWFLLANDFASYLKAQEEVDACYKDQSEWLRRSI MYTAGSGKFSSDRTIREYAEDIWHVK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 872 Download |
| MAYQQLQGYR VAGAPPVSRQ FAPRVGSGRR ALRVHAVAEL DKTAPIVRGG TSSVPAPADI 60 ANKLRYLFGR NGDYTTADAY QGTAWSVREK LIDSFNKTHE YWKKEDPKFV YYLSAEFLMG 120 RSLINTVYNL GLEGEYAEAL NQMGYEMERV ADAERDAALG NGGLGRLAAC FLDSMATLDL 180 PGWGYGIRYK YGMFKQALKN GYQVELPDIW LTKGNPWELR RDDVKYEVGF GGRVERRKQG 240 SKEVTVWTPS ERVIAQAYDN PIPGYNTPTT SNLRLWDAVP VTEFDLGAFN AGDYDRAMLE 300 RERAEGISAV LYPNDSTPEG KELRLKQQYF FVCASLQDVL SRFKAVHATD FNLLPEKACF 360 QLNDTHPTIA VAELMRLLVD VEGLDWDQAW TITTKCLNYT NHTVMPEALE KWPVKVMAKM 420 LPRHMEIIEV INEGWTKWLA GHLKDLKPEE RAKRVAAMSI IHENPWNKDE MLVNMAYLAV 480 VGSSAVNGVA AIHSNIVKDE ILNDFYQIFP SKFQNKTNGV TPRRWLAWCN PELAALITDA 540 LGTSEWINDT EKLAGLRAFA SDKSFQAKWS AVKKAKKAKL AQLIKKVHGD DVNQEALFDI 600 QIKRIHEYKR QYLNVLSIIW RYKQLKKMSP EERKKAVPRV CVIGGKAASA YDMAKRIIRL 660 VTAVGDVINK DPDTQDYLRL YFLPDYNVSL AETIIPAAEL SQHISTAGTE ASGTSNMKFQ 720 MNGCLIIGTW DGANIEIAEE TGIENVFVFG VRAEEINQLR KERKNLKTDP RWDELMRDIE 780 SGMFGDKDYF KPLVDSVNNM KVGNDWFLLA NDFASYLKAQ EEVDACYKDQ SEWLRRSIMY 840 TAGSGKFSSD RTIREYAEDI WHVKPSRPTI A* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 58 | 863 | 813 | + 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 | 60 | 863 | 811 | + 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 | 139 | 865 | 738 | + 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 | 60 | 867 | 817 | + glycogen phosphorylase; Provisional | ||
| COG0058 | GlgP | 0 | 59 | 865 | 819 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
| 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 | ABB88567.1 | 0 | 59 | 867 | 196 | 995 | PhoB [Chlamydomonas reinhardtii] |
| GenBank | EEH55145.1 | 0 | 60 | 867 | 209 | 1008 | glycosyltransferase family 35 protein [Micromonas pusilla CCMP1545] |
| RefSeq | XP_001694015.1 | 0 | 59 | 867 | 196 | 995 | starch phosphorylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700091.1 | 0 | 1 | 869 | 1 | 871 | starch phosphorylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002505241.1 | 0 | 60 | 867 | 86 | 883 | glycosyltransferase family 35 protein [Micromonas sp. RCC299] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2ffr_A | 0 | 75 | 867 | 36 | 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 | 3t3i_A | 0 | 75 | 867 | 47 | 831 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| PDB | 3t3h_A | 0 | 75 | 867 | 47 | 831 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| PDB | 3t3g_A | 0 | 75 | 867 | 47 | 831 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| PDB | 3t3e_A | 0 | 75 | 867 | 47 | 831 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO586252 | 551 | 315 | 865 | 0 |
| FC108203 | 277 | 588 | 863 | 0 |
| HO418036 | 538 | 270 | 787 | 0 |
| FC081954 | 260 | 611 | 869 | 0 |
| FD818102 | 249 | 123 | 371 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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