y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000281786 |
Family | CBM45 |
Protein Properties | Length: 2070 Molecular Weight: 229734 Isoelectric Point: 7.6031 |
Chromosome | Chromosome/Scaffold: 00739658 Start: 14993 End: 39719 |
Description | alpha-amylase-like 3 |
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 |
CBM45 | 1467 | 1543 | 1.3e-22 |
VHWGVCRDDAKRWEIPAAPHPPETVVFKDKALRTRLQQREDGNGCSGLFTLEEGLAGFLFVFKLNETMWLNCVGNDF | |||
GH13 | 1681 | 1971 | 5.9e-37 |
KSKAAELSSLGFTVIWFPPPTDSVSPQGYMPRDLYNMNSRYGNMDELKETVKTFHDAGLKVLGDAVLNHRCAEYQNQNGVWNIFGGRLNWDERAVVADDP HFQGRGNKSSGDSFHAAPNIDHSQDFVRKDIREWLCWLRDDIGYDGWRLDFVRGFWGGYVKDYMDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVD WINATNGTCGAFDVTTKGILHAALERCEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPNKKEMQGYAYILTHPGTPTVFY |
Full Sequence |
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Protein Sequence Length: 2070 Download |
MGLKAEDGKV EAWDISKSKV RRKKKHKADG DDDDDVEEEG SGCWVRLRFF GSCISSRSKV 60 DSSTSGTSAT HCGEIKSIND TSRDQPTATV VSSSTTSNTE SNASTSKLEE ELKVASRLRK 120 FTFIDLKLAT RNFRPESLLG EGGFGCVFKG WIEENGTAPV KPGTGLTVAV KTLNHDGLQG 180 SLPLPWSIRM KIALGAAKGL AFLHEEAERP VIYRDFKTSN ILLDADYNAK LSDFGLAKDG 240 PEGDKTHVST RVMGTYGYAA PEYVMTEVIL PLSGSECYLQ ELGLKTVAAI SAHPVGHYVV 300 DVRHLTSKSD VYSFGVVLLE MLTGRRSMDK NRPNGEHNLV EWARPHLGER RRFYRLIDPR 360 LEGHFSIKGV QKAAQLAAHC LSRDPKARPL MSEVVEALKP LPALKDMASS SYYFQTMQGD 420 RVGSSPNTRN GVRPQGGLLT RNGHNQQRSL SIPNGTHASP YHLQHPQPSP KPNGKSKWDK 480 FLVVFKWTSL LLLSGKLLGS SMMCLNLAVT VCHGVWGSQI AGHLSLRVQQ LDVRCETKTK 540 DNVFVTVVAS VQYRALAEKA SDAFYKLSNT RGQIQSYVFD VIRASVPKLD LDSTFEQKND 600 IAKAVEDELA KAMSHYGFEI VQTLIVDIEP DEHVKRAMNE INAAARMRLA ATEKAEAEKI 660 LQIKRAEGEA ESKYLSGLGI ARQRQAIVDG LRDSVLAFSE NVPGTSSKDV MDMVLVTQYF 720 DTLKDIGASS KSNSVFIPHG PGAVKDISSQ IRDGLLQGSR QRVTEQHLKA EYARSNLSYD 780 SRGHQSTEPL LQINGHKPVP LPRTGSNGPR LSSQSQQSPF FGGPGLYLDI GKKARDLLYK 840 DYQSDHKFTV TTYTSTGVHG FSPVYVKLIL QCHCICNFVF SVALVEFMVF QLALSRICAN 900 GMAISSTGIR KGDLYLGDVS TQLKNKNITT DVKVDTNSNV ITTITVDEPS PGLKAIFSFI 960 APDQRSGKVE LQYQHEYAGI STSIGLTANP IVHFSGVVGN NLLSLGTDLS FDTASGNFTK 1020 VNAGLNFTHS DLIASLLLND KADTITASYY HTVSPLTNTA VGAELSHSFS SNENSLTIGT 1080 AHALDPLTTV KARVNNYGRA SALIQHEWRP KSFFTISGEV DTRAIEKSAK DRALLHHYRR 1140 QKPSHRLPPS KHPLKLSSSF TAFPKKLVVS NGRSFCNFQP PTLSVRAAST DTATVEATEF 1200 ADAFYKETFP LKRTEVVEGK MIVKLDNGKD AKNWVLTVGC NLPGKWVLHW GVNYVDDVGS 1260 EWDQPPSEMR PAGSVSIKVR IWVLKFDCRA VGWHEFNIRV DFQDYAIETP LKESLSPVGG 1320 DTSHEVKIDV TPNSAIAAIN FVLKDEETGA WYQHRGRDFK VPFVGYLQDD DNVVGATRAL 1380 GAWSGTLGKL SNVFVKAETS NSKDQESSSE SRDPQQKTMR LEGFYEELPI AKEIAVNHSA 1440 TVSVRKCPET TKNLLYLETD LPDHAVVHWG VCRDDAKRWE IPAAPHPPET VVFKDKALRT 1500 RLQQREDGNG CSGLFTLEEG LAGFLFVFKL NETMWLNCVG NDFYIPLLSS NNSIAVQNEV 1560 QSEDAQVPDR SRETNFTAYT DGIINEIRNL VSDISSEKSQ RKRSKEAQET ILQEIEKLAA 1620 EAYSIFRTTV PTLPEEIIAE TEKVKVAPAK ICSGTGTGFE ILCQGFNWES SKSGRWYEEL 1680 KSKAAELSSL GFTVIWFPPP TDSVSPQGYM PRDLYNMNSR YGNMDELKET VKTFHDAGLK 1740 VLGDAVLNHR CAEYQNQNGV WNIFGGRLNW DERAVVADDP HFQGRGNKSS GDSFHAAPNI 1800 DHSQDFVRKD IREWLCWLRD DIGYDGWRLD FVRGFWGGYV KDYMDASEPY FAVGEYWDSL 1860 SYTYGEMDHN QDAHRQRIVD WINATNGTCG AFDVTTKGIL HAALERCEYW RLSDEKGKPP 1920 GVLGWWPSRA VTFIENHDTG STQGHWRFPN KKEMQGYAYI LTHPGTPTVF YDHIFSHYQS 1980 EIAALISLRN RNKLNCRSRV KITKAERDVY AAIIDEKVAI KIGPGTVDAQ LRTRRASLLQ 2040 QHRIAASRLS VEVVSMVLGS KGSAPSYTHC 2100 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd03407 | Band_7_4 | 5.0e-121 | 512 | 752 | 243 | + A subgroup of the band 7 domain of flotillin (reggie) like proteins. This subgroup contains proteins similar to stomatin, prohibitin, flotillin, HlfK/C and podicin. Many of these band 7 domain-containing proteins are lipid raft-associated. Individual proteins of this band 7 domain family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podicin gene give rise to autosomal recessive steroid resistant nephritic syndrome. | ||
PLN00196 | PLN00196 | 1.0e-130 | 1660 | 2024 | 378 | + alpha-amylase; Provisional | ||
PLN02361 | PLN02361 | 5.0e-156 | 1658 | 2026 | 375 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-160 | 1661 | 2000 | 343 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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. | ||
PLN02784 | PLN02784 | 0 | 1133 | 2025 | 897 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0004672 | protein kinase activity |
GO:0005509 | calcium ion binding |
GO:0005524 | ATP 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 |
GenBank | AAX33231.1 | 0 | 1134 | 2025 | 9 | 875 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1169 | 2038 | 39 | 882 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1134 | 2038 | 9 | 872 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1134 | 2038 | 9 | 888 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1156 | 2025 | 27 | 875 | alpha-amylase, 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 | 2qpu_C | 0 | 1660 | 2024 | 2 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 1660 | 2024 | 2 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 1660 | 2024 | 2 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 1660 | 2023 | 2 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 1660 | 2023 | 2 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |