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Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra009461 |
Family | GH13 |
Protein Properties | Length: 1335 Molecular Weight: 148552 Isoelectric Point: 5.836 |
Chromosome | Chromosome/Scaffold: 10 Start: 16749128 End: 16758413 |
Description | limit dextrinase |
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 |
GH13 | 363 | 770 | 1.8e-31 |
DCAGVKHLQKLADAGLTHLHLLPTYQFGDVDDEKETWKYIDTSVLEGLPPDSAEAQARITEIQNDDGFNWGYNPVLWGVPKGSYASDPTGPCRIIEFRKM VQALNHVGLNVVLDVVYNHLHANGPHDKDSVLDKIVPGYYLRRNNDGFIENSTCVNNTASEHYMVDRLIRDDLLNWVVNYKVDGFRFDLMGHIMKDTMVN AKSAIGNLRKETDGVDGSRIYIYGEGWNFGEVANNGRGVNASQFNLTGTGIGSFNDRIRDATLGGSPFGHPLQQGFITGLLLQPNGHDHGSEATQQLMLS TAKDHIQIGMAANLKDYVLTNHEGKEVKGSEILMHDATPVAYASEPTETINYVSAHDNETLFDIISLKTPMEISVDERCRINHLASSMISLSQGIPFFHA GDEILRSK |
Full Sequence |
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Protein Sequence Length: 1335 Download |
MALTLLTLTT SVPLLSRIFA AAFPLRSRFR RPSSSISRFQ LGFPSTTHRS ESLRCLCSSS 60 SSAASPMQFE VSTPNSQFLD SLLYSRAYWV TEGVIAWNVD VGEGSCYLYA SRVAGLSFSE 120 DGIDGFDFRV KLEAESGSLR TNVVEKFPHI GNYKPFKVPS DLEVKDLVKS QLAIVCFDAE 180 GRLIDGTGLQ LPGVLDELFS YDGPLGANFT PGGGVSLHLW APTAQEVTVC IYKNPLDKSP 240 METCPLEEVN GVWSIQGPSS WEGCYYVYKV SVYHPSTLKV ETCYANDPYA RGLSADASKT 300 YLVNLDSDDL KPEGWEKLAD KKPCLRSYSD ISIYELHVRD FSVYDETVEP EHRGGYLAFT 360 LKDCAGVKHL QKLADAGLTH LHLLPTYQFG DVDDEKETWK YIDTSVLEGL PPDSAEAQAR 420 ITEIQNDDGF NWGYNPVLWG VPKGSYASDP TGPCRIIEFR KMVQALNHVG LNVVLDVVYN 480 HLHANGPHDK DSVLDKIVPG YYLRRNNDGF IENSTCVNNT ASEHYMVDRL IRDDLLNWVV 540 NYKVDGFRFD LMGHIMKDTM VNAKSAIGNL RKETDGVDGS RIYIYGEGWN FGEVANNGRG 600 VNASQFNLTG TGIGSFNDRI RDATLGGSPF GHPLQQGFIT GLLLQPNGHD HGSEATQQLM 660 LSTAKDHIQI GMAANLKDYV LTNHEGKEVK GSEILMHDAT PVAYASEPTE TINYVSAHDN 720 ETLFDIISLK TPMEISVDER CRINHLASSM ISLSQGIPFF HAGDEILRSK SLDRDSYNSG 780 DWFNRLDFSY NSNNWGVGLP PKGKNEHSWP LIKPRLQDPS FKPQSSHIVA TLNSFLDLLR 840 IRYSSPLFRL DTAKAIQDRV RFHNTGPSSV PGAIIMSIED GHKGITSVSQ IDPVYSFIVV 900 IFNARPSEFS FFSPALKDRN LELHPIQVKS GDEIVRKSVY DAFSGGFTVP ARTTTVCDEQ 960 SGNEMNKGDE ESSNYTDVSI LSMRGGDGHN SYATNSLLQR RVLSMSKSIL VKNTKEMVTN 1020 LDFPKCIKVA DLGCSSGQNT FLAMSEIVNT INALCQERNQ IPPEIDCCLN DLPGNDFNTT 1080 FKFISFFNEK LTSNTLCFVS GVPGSFHSRL FPSKSLHFIH SNCSVNYLSK VPEGLEKNKM 1140 SVYITSSSPL SEYKAYLNQF QKDFTTFLRM RSEEMVSNGR MVITLLGRNA IDDPLYRDCC 1200 HHLTLLSDSL RDLVFEGLVS ASKVISFNMP LYDPTDEELK EIIRNEGTFQ INDLETHAFD 1260 LGHSKEENRE SCRAKPGEKE ANCIRAAFEM MLVAHFGDAI NIDTLFAKYA HHVSQHASCM 1320 RKTSVILVVS LVRK* 1380 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02104 | pulA_typeI | 2.0e-132 | 196 | 930 | 751 | + pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. | ||
pfam03492 | Methyltransf_7 | 5.0e-140 | 1010 | 1334 | 336 | + SAM dependent carboxyl methyltransferase. This family of plant methyltransferases contains enzymes that act on a variety of substrates including salicylic acid, jasmonic acid and 7-Methylxanthine. Caffeine is synthesised through sequential three-step methylation of xanthine derivatives at positions 7-N, 3-N, and 1-N. The protein 7-methylxanthine methyltransferase (designated as CaMXMT) catalyzes the second step to produce theobromine. | ||
cd11341 | AmyAc_Pullulanase_LD-like | 2.0e-160 | 330 | 794 | 475 | + Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. | ||
PLN02877 | PLN02877 | 0 | 66 | 956 | 891 | + alpha-amylase/limit dextrinase | ||
TIGR02103 | pullul_strch | 0 | 82 | 956 | 910 | + alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102) [Energy metabolism, Biosynthesis and degradation of polysaccharides]. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0008168 | methyltransferase activity |
GO:0043169 | cation binding |
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 | CBI31395.1 | 0 | 23 | 956 | 24 | 949 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196056.2 | 0 | 1 | 959 | 1 | 961 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
Swiss-Prot | Q8GTR4 | 0 | 1 | 959 | 1 | 961 | PULA1_ARATH RecName: Full=Pullulanase 1, chloroplastic; Short=AtPU1; AltName: Full=Protein LIMIT DEXTRINASE; Short=AtLDA; Flags: Precursor |
RefSeq | XP_002315334.1 | 0 | 67 | 959 | 1 | 891 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532780.1 | 0 | 53 | 960 | 62 | 963 | pullulanase, 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 | 4aio_A | 0 | 85 | 959 | 6 | 881 | A Chain A, Crystal Structure Of L-serine-o-acetyltransferase Found In D- Cycloserine Biosynthetic Pathway |
PDB | 2y5e_A | 0 | 85 | 959 | 6 | 881 | A Chain A, Crystal Structure Of L-serine-o-acetyltransferase Found In D- Cycloserine Biosynthetic Pathway |
PDB | 2y4s_A | 0 | 85 | 959 | 6 | 881 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhf_A | 0 | 87 | 968 | 179 | 1077 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
PDB | 2fhc_A | 0 | 87 | 968 | 179 | 1077 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1824 | EC-3.2.1.41 | pullulanase |