Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_27.5 |
Family | GT35 |
Protein Properties | Length: 1018 Molecular Weight: 115312 Isoelectric Point: 6.1132 |
Chromosome | Chromosome/Scaffold: 27 Start: 29406 End: 44990 |
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 | 343 | 1011 | 0 |
RTYGLRYQYGLFRQVILDGFQHEQPDYWLNFGNPWEIERVHVSYTVKFYGIVEEELLNGEKFQVWVPGETVEAVAYDNPIPGFGTRNTINLRLWAAKPSD QSDMESYNTGDYINAIVNRQRAETISSVLYPDDRSYQGKELRLKQQYFFVSASLQDIIRRYKDSHNNFDDFEEKVALQLNDTHPSLAIAEVMRILIDEEH LGWDIAWNIVLKIFSFTTHTVSSAGLEKIPVDLLGTLLPRHLQIIYDINFNFMEDLKKRIGLDYDRLSRMSIVEEGAVKNIRMANLSVVCSHTVNGVSRM HSELLKTRVFKDFYELWPQKFQYKTNGVTQRRWIVVSNPSLCILISKWLGTEAWIRDIDLLAGLQEYAKSLELHQEWKMVRKVNKMRLAEYIEAMSGVKV SPDAMFDVQIKRIHEYKRQLLNILGIIHRYDCIKNMEKSERRKVVPRVCIIGGKAAPGYEIAKKIIKLCHAVAEMINNDADVGDLIKLVFIPDYNVSVAE LVIPAADLSQHISTAGHEASGTGSMKFLMNGCLLLATADGSTLEIIEEIGEDNMFLFGAKMHEVPALREEGSTLKVPLQFARVVRMVRDGYFGYQEYFRS LCDSIDGGGDFYLLGSDFESYLEAQAAADKTFVDQEKWTEMSILSTARSSRFSSDRTIEEYAAETWGIE |
Full Sequence |
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Protein Sequence Length: 1018 Download |
MTSLTLPLQA IALHQSKLPF ASAPNRFSTP SSRTFFALPL VYKSIKLTSP AFASTGDSSL 60 HSTSVTVDAE DPAADTATEF VIRTRNRIGL LQVITRVFNV LGLLVDRAAI ELEGDFFVQR 120 FYVTDSHGNK IDGQDNIDRI KRALFEAIDS GGDGTTGTSV AVAPAGRGLV VRRAGFGLGL 180 GDGSAKAERM FGLMDAFLKN DPVSLQKDIL HHVEYTVARS RFSFDDFEAY QALAHSVRDR 240 LIERWHDTQM HFKRKDPKRL YFLSLEFLMG RSLSNSVINL GIKDQYADAL SQLGFEFEVV 300 AEQEGDAALW QWWPCSSLSM SNGFSGNFGL SCMGIKCNER YRRTYGLRYQ YGLFRQVILD 360 GFQHEQPDYW LNFGNPWEIE RVHVSYTVKF YGIVEEELLN GEKFQVWVPG ETVEAVAYDN 420 PIPGFGTRNT INLRLWAAKP SDQSDMESYN TGDYINAIVN RQRAETISSV LYPDDRSYQG 480 KELRLKQQYF FVSASLQDII RRYKDSHNNF DDFEEKVALQ LNDTHPSLAI AEVMRILIDE 540 EHLGWDIAWN IVLKIFSFTT HTVSSAGLEK IPVDLLGTLL PRHLQIIYDI NFNFMEDLKK 600 RIGLDYDRLS RMSIVEEGAV KNIRMANLSV VCSHTVNGVS RMHSELLKTR VFKDFYELWP 660 QKFQYKTNGV TQRRWIVVSN PSLCILISKW LGTEAWIRDI DLLAGLQEYA KSLELHQEWK 720 MVRKVNKMRL AEYIEAMSGV KVSPDAMFDV QIKRIHEYKR QLLNILGIIH RYDCIKNMEK 780 SERRKVVPRV CIIGGKAAPG YEIAKKIIKL CHAVAEMINN DADVGDLIKL VFIPDYNVSV 840 AELVIPAADL SQHISTAGHE ASGTGSMKFL MNGCLLLATA DGSTLEIIEE IGEDNMFLFG 900 AKMHEVPALR EEGSTLKVPL QFARVVRMVR DGYFGYQEYF RSLCDSIDGG GDFYLLGSDF 960 ESYLEAQAAA DKTFVDQEKW TEMSILSTAR SSRFSSDRTI EEYAAETWGI EPCRCPF* 1020 |
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 | 206 | 1010 | 827 | + 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 | 209 | 1010 | 823 | + 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 | 289 | 1012 | 741 | + 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 | 204 | 1014 | 826 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 204 | 1012 | 829 | + 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 | 194 | 1016 | 1 | 813 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001757919.1 | 0 | 194 | 1013 | 1 | 810 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 190 | 1016 | 1 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 190 | 1017 | 1 | 818 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509431.1 | 0 | 1 | 1017 | 1 | 949 | 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 | 200 | 1013 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 200 | 1013 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1abb_D | 0 | 205 | 1014 | 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 | 205 | 1014 | 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 | 205 | 1014 | 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 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779924 | 637 | 98 | 724 | 0 |
HO586252 | 541 | 475 | 1013 | 0 |
HO376977 | 448 | 572 | 1018 | 0 |
HO417459 | 285 | 626 | 910 | 0 |
HO417459 | 212 | 427 | 632 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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