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Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa000587m |
Family | GT35 |
Protein Properties | Length: 1087 Molecular Weight: 122224 Isoelectric Point: 6.81 |
Chromosome | Chromosome/Scaffold: 4 Start: 2519026 End: 2527566 |
Description | alpha-glucan phosphorylase 2 |
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 | 367 | 1078 | 0 |
ALSQLGFEFEVLAEQEGDAALGNGGLARLSACQMDSMATLDYPAWGYGLRYEYGLFRQVILDGFQHEQPDFWLNFGNPWETERVHVTYPVKFYGVVEEEN LNGEKCNVWIPGEVVEAVAYDNPIPGYGTRNTITLRLWAGKPSDQHDMEAYNTGDYINAVVCRQKAENISSVLYPDDRSFQGKELRLKQQYFFVSASIQD IIRRFKEAHSNFDEFPEKVALQLNDTHPSLAIAEVMRVLVDKEHLGWNKAWDIACKIFSFTIHAVIAEGLEKIPVDLLGSLLPRHLQIIYEINFKFVEEL KKRIGLDYNRLSRMSIIEEGAVKSIRMANLAIVCSHTVNGVSEVHSELLKAKLFKDFYELWPQKFQCKTNGVTQRRWIVVSNPSLCALISKWLGTEAWIR DVDLLTGLRAYAADPDLQQEWMMVKKVNKMRLAEYIEAMSGVKVSLDAMFDVQTKRIHEYKRQLLNILGIIHRYDCIKNMEKSQRSKVVPRVCIIGGKAA PGYEIAKKIIKLCHAVAEKINNDTDVGDLLKLVFIPDYNVSVAELVIPGADLSQHISTAGHEASGTGSMKFLMNGCLLLATEDGSTVEIVEEIGADNLFL FGAKIHEVPNLREEGSPKMPLQCARVIRMVRDGYFGFKDYFESLCDTVDGGKDFYLVGSDFESYLEAQAAADKAFADPSKWTQMSILSTAGSGRFSSDRT IRDYAEKTWGIE |
Full Sequence |
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Protein Sequence Length: 1087 Download |
MRLSTWYPHP VPSKSEKSRK SLFPTITVSH SQTHCDCTQS SIFFFFFHLQ TPKLSLPESF 60 STCECDSSKS PHSTMLTLSS RLFTITDQSK LASSSSTFLF PLFPSHSRSF SRSSRSSILY 120 GRTHVAKPIR ASASQLPSAA SSVTVENSES ESDPSCTLFV IRARNRIGLL QVITGVFKVL 180 GLHVEKATVE FEGDFFVKRF FVTDSHGAKI ADPDSLDRIK KALTDAIEDG GTVSMGPASP 240 TTRGVMVRRP GSGLGMSLGS DSAKAERMFR LMDGFLKNDS ISLQQDILRH VEYTVARSRF 300 NFDDFEAYQA LAHSVRDRLI ERSHDTQLYF KRKDPKRVYF LSFEYLMGRS LSNSVINLGI 360 RDQYADALSQ LGFEFEVLAE QEGDAALGNG GLARLSACQM DSMATLDYPA WGYGLRYEYG 420 LFRQVILDGF QHEQPDFWLN FGNPWETERV HVTYPVKFYG VVEEENLNGE KCNVWIPGEV 480 VEAVAYDNPI PGYGTRNTIT LRLWAGKPSD QHDMEAYNTG DYINAVVCRQ KAENISSVLY 540 PDDRSFQGKE LRLKQQYFFV SASIQDIIRR FKEAHSNFDE FPEKVALQLN DTHPSLAIAE 600 VMRVLVDKEH LGWNKAWDIA CKIFSFTIHA VIAEGLEKIP VDLLGSLLPR HLQIIYEINF 660 KFVEELKKRI GLDYNRLSRM SIIEEGAVKS IRMANLAIVC SHTVNGVSEV HSELLKAKLF 720 KDFYELWPQK FQCKTNGVTQ RRWIVVSNPS LCALISKWLG TEAWIRDVDL LTGLRAYAAD 780 PDLQQEWMMV KKVNKMRLAE YIEAMSGVKV SLDAMFDVQT KRIHEYKRQL LNILGIIHRY 840 DCIKNMEKSQ RSKVVPRVCI IGGKAAPGYE IAKKIIKLCH AVAEKINNDT DVGDLLKLVF 900 IPDYNVSVAE LVIPGADLSQ HISTAGHEAS GTGSMKFLMN GCLLLATEDG STVEIVEEIG 960 ADNLFLFGAK IHEVPNLREE GSPKMPLQCA RVIRMVRDGY FGFKDYFESL CDTVDGGKDF 1020 YLVGSDFESY LEAQAAADKA FADPSKWTQM SILSTAGSGR FSSDRTIRDY AEKTWGIEPC 1080 RFPSDG* 1140 |
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 | 284 | 1077 | 801 | + 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 | 287 | 1077 | 802 | + 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 | 367 | 1079 | 720 | + 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 | 314 | 1081 | 782 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 282 | 1079 | 812 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
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 | 272 | 1084 | 1 | 814 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001757919.1 | 0 | 272 | 1080 | 1 | 810 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 268 | 1084 | 1 | 818 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 268 | 1083 | 1 | 817 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509431.1 | 0 | 144 | 1083 | 63 | 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 | 278 | 1080 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 278 | 1080 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1abb_D | 0 | 283 | 1081 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
PDB | 1abb_C | 0 | 283 | 1081 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
PDB | 1abb_B | 0 | 283 | 1081 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779924 | 619 | 177 | 792 | 0 |
HO586252 | 541 | 543 | 1080 | 0 |
HO376977 | 446 | 640 | 1083 | 0 |
HO417459 | 293 | 694 | 986 | 0 |
HO417459 | 212 | 495 | 700 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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