| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G141399_T02 |
| Family | CBM53 |
| Protein Properties | Length: 1639 Molecular Weight: 183739 Isoelectric Point: 4.6874 |
| Chromosome | Chromosome/Scaffold: 10 Start: 59506710 End: 59518288 |
| Description | starch synthase 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 |
| CBM53 | 792 | 875 | 8.6e-33 |
| STIDLYFNRDLSAVANEPDVLIKGAFNGWKWRFFTEKLHKSELAGDWWCCKLYIPKQAYRMDFVFFNGHTVYENNNNNDFVIQI | |||
| CBM53 | 1128 | 1216 | 5.3e-34 |
| GTTIDVLYNPSNTVLTGKPEVWFRCSFNRWMYPGGVLPPQKMVQAENGSHLKVTVYVPRDAYMMDFVFSESEEGGIYDNRNGLDYHIPV | |||
| CBM53 | 967 | 1055 | 1.1e-34 |
| ATVRLYYNINSRPLVHSTEIWMHGGYNNWIDGLSFAERLVHHHDKDCDWWFVDVVVPERTYVLDWVFADGPPGSARNYDNNGGHDFHAT | |||
| GT5 | 1227 | 1591 | 0 |
| HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHIHQSFSWGGSEIKVWRGLVEGLCVYFLEPQNGMFGVGYVYGRDDD RRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANARVVFTIHNLEFGAHHIGKAMRYCDKATTVSNTYSKEVSGHGAIVPHLGKF YGILNGIDPDIWDPYNDNFIPVHYTCENVVEGKRAAKRALQQKFGLQQIDVPVVGIVTRLTAQKGIHLIKHAIHRTLERNGQVVLLGSAPDSRIQADFVN LANKLHGVNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGL | |||
| Full Sequence |
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| Protein Sequence Length: 1639 Download |
| MEMVLRSQSP LCLRSGPVLI FRPTVAGGGG GTQSLLRTTR FARRRVIRCV VASPGCPNRK 60 SRTASPNVKV AAYSNYAPRL LVESSSKKSE HHDSSRHREE TIDTYNGLSG SDAAELTSNR 120 DVEIEVDLQH ISEEELPGKV SINASLGEME TVDEAEVEED KFEVDTSGIV LRNVAVREVD 180 PKDEHNAKDV FVVDSSGTAP DNAAVEEVVD EAEVEEDMVD VDILGLDLNN ATIEEIDLME 240 EALLENFDVD SPGNASSGRT YGGVDELGEL PSTSVDCIAI NGKRRSLKPK PLPIVRFQEQ 300 EQIVLSIVDE EGLIASSCEE GQPVVDYDKQ EENSTAFDEQ KQLTDDFPEE GISIVHFPEP 360 NNDIVGSSKF LEQKQELDGS YKQDRSTTGL HEQDQSVVSS HGQDKSIVGV PQQIQYNDQS 420 IAGSHRQDQS IAGAPEQIQS VAGYIKPNQS IVGSCKQHEL IIPEPKKIES IISYNEIDQS 480 IVGSHKQDKS VVSVPEQIQS IVSHSKPNQS TVDSYRQAES IIGVPEKVQS ITSYDKLDQS 540 IVGSLKQDEP IISVPEKIQS IVHYTKPNQS IVGLPKQQQS IVHIVEPKQS IDGFPKQDLS 600 IVGISNEFQT KQLATVGTHD GLLMKGVEAK ETSQKTEGDT LQATFNVDNL SQKQEGLTKE 660 ADEITIIEKI NDEDLVMIEE QKSIAMNEEQ TIVTEEDIPM AKVEIGIDKA KFLHLLSEEE 720 SSWDENEVGI IEADEQYEVD ETSMSTEQDI QESPNDDLDP QALWSMLQEL AEKNYSLGNK 780 LFTYPDVLKA DSTIDLYFNR DLSAVANEPD VLIKGAFNGW KWRFFTEKLH KSELAGDWWC 840 CKLYIPKQAY RMDFVFFNGH TVYENNNNND FVIQIESTMD ENLFEDFLAE EKQRELENLA 900 NEEAERRRQT DEQRRMEEER AADKADRVQA KVEVETKKNK LCNVLGLARA PVDNLWYIEP 960 ITTGQEATVR LYYNINSRPL VHSTEIWMHG GYNNWIDGLS FAERLVHHHD KDCDWWFVDV 1020 VVPERTYVLD WVFADGPPGS ARNYDNNGGH DFHATLPNNM TEEEYWMEEE QRIYTRLQQE 1080 RREREEAIKR KAERNAKMKA EMKEKTMRMF LVSQKHIVYT EPLEIHAGTT IDVLYNPSNT 1140 VLTGKPEVWF RCSFNRWMYP GGVLPPQKMV QAENGSHLKV TVYVPRDAYM MDFVFSESEE 1200 GGIYDNRNGL DYHIPVFGSI AKEPPMHIVH IAVEMAPIAK VGGLGDVVTS LSRAVQDLGH 1260 NVEVILPKYG CLNLSNVKNL HIHQSFSWGG SEIKVWRGLV EGLCVYFLEP QNGMFGVGYV 1320 YGRDDDRRFG FFCRSALEFL LQSGSSPNII HCHDWSSAPV AWLHKENYAK SSLANARVVF 1380 TIHNLEFGAH HIGKAMRYCD KATTVSNTYS KEVSGHGAIV PHLGKFYGIL NGIDPDIWDP 1440 YNDNFIPVHY TCENVVEGKR AAKRALQQKF GLQQIDVPVV GIVTRLTAQK GIHLIKHAIH 1500 RTLERNGQVV LLGSAPDSRI QADFVNLANK LHGVNHGQVR LSLTYDEPLS HLIYAGSDFI 1560 LVPSIFEPCG LTQLVAMRYG TIPIVRKTGG LISRAAARQG SSTLSSMWTM TRNEPEIEAL 1620 SPTGLALTEL IATVLTTR* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR02095 | glgA | 7.0e-118 | 1226 | 1591 | 409 | + glycogen/starch synthase, ADP-glucose type. This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| PRK00654 | glgA | 9.0e-129 | 1226 | 1591 | 404 | + glycogen synthase; Provisional | ||
| cd03791 | GT1_Glycogen_synthase_DULL1_like | 5.0e-137 | 1227 | 1592 | 412 | + This family is most closely related to the GT1 family of glycosyltransferases. Glycogen synthase catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms. | ||
| PLN02316 | PLN02316 | 0 | 679 | 1591 | 922 | + synthase/transferase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0009058 | biosynthetic process |
| GO:2001070 | starch binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAF87999.1 | 0 | 1 | 1591 | 1 | 1545 | AF258608_1 starch synthase III [Triticum aestivum] |
| GenBank | AAF88000.1 | 0 | 1 | 1591 | 1 | 1528 | starch synthase III [Aegilops tauschii] |
| GenBank | ACC86846.1 | 0 | 1 | 1592 | 1 | 1602 | starch synthase IIIa precursor [Sorghum bicolor] |
| RefSeq | NP_001104881.1 | 0 | 1 | 1592 | 1 | 1592 | starch synthase DULL1 [Zea mays] |
| RefSeq | XP_002443985.1 | 0 | 1 | 1592 | 1 | 1582 | hypothetical protein SORBIDRAFT_07g005400 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3d1j_A | 0 | 1226 | 1591 | 1 | 401 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 3cx4_A | 0 | 1226 | 1591 | 1 | 401 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 3cop_A | 0 | 1226 | 1591 | 1 | 401 | A Chain A, Crystal Structure Of E.Coli Gs Mutant E377a In Complex With Adp And Acceptor Analogue Heppso |
| PDB | 3guh_A | 0 | 1226 | 1591 | 1 | 401 | A Chain A, Crystal Structure Of E.Coli Gs Mutant E377a In Complex With Adp And Acceptor Analogue Heppso |
| PDB | 2r4u_A | 0 | 1226 | 1591 | 1 | 401 | A Chain A, Crystal Structure Of E.Coli Gs Mutant E377a In Complex With Adp And Acceptor Analogue Heppso |
| Hydropathy |
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