Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | AC235664_4.1 |
Family | AA2 |
Protein Properties | Length: 848 Molecular Weight: 92492.5 Isoelectric Point: 6.3869 |
Chromosome | Chromosome/Scaffold: 2356644 Start: 14803 End: 18138 |
Description | OPC-8:0 CoA ligase1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 34 | 308 | 0 |
FEKIVRENIFNKQSASPATAPGLLRLFFHDCITDGCDGSVLISSTAYNPHAEKDAEINLSLSGDGYDVVNKIKNALEIACPGVVSCSDIVAQATRDLVKM VGGPFYPVALGRKDSRVSEASRTEKALPTTKMTMDDIISKFTVKNFTIKEMVALTGAHTIGFTHCKEFSDRIFNFSKTSETDPTLHPKLAKGLREVCKNY TTDPNMAAFNDVRSPGKFDNAYYQNVLKGLGLLRTDAMLGSDPRTKPIVELYARDEQAFFQDFARAMEKVSVLGV |
Full Sequence |
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Protein Sequence Length: 848 Download |
MAFPILFLLL ISLPFSFSSA ELNIDYYKQT CPDFEKIVRE NIFNKQSASP ATAPGLLRLF 60 FHDCITDGCD GSVLISSTAY NPHAEKDAEI NLSLSGDGYD VVNKIKNALE IACPGVVSCS 120 DIVAQATRDL VKMVGGPFYP VALGRKDSRV SEASRTEKAL PTTKMTMDDI ISKFTVKNFT 180 IKEMVALTGA HTIGFTHCKE FSDRIFNFSK TSETDPTLHP KLAKGLREVC KNYTTDPNMA 240 AFNDVRSPGK FDNAYYQNVL KGLGLLRTDA MLGSDPRTKP IVELYARDEQ AFFQDFARAM 300 EKVSVLGVKT GTQGEVRSRC DQFNKIQDLN TATLVLSQFS QGDLADARIA FIDLNTDHSV 360 TYGEIRRSVY SLATALFHGL EIRKGDVVFL LSPNSILYST ICLAVLSVGA ILTTANPLNT 420 KSEIAKQVHD SGAKLAISAP EELHKLVPTG VPTILTSGTS DGKFLSVEEL IEGCYDSHEL 480 PHVPVEQSDT AAILYSSGTT GVSKGVVLTH ANLITIMKLL CWSADVSTAQ DDVFLAFIPM 540 FHVYGLMFFG FGLLCVGVTT VLMQKYDFQA MLVAIEKHKI NNIPAVPPVI HSLVKHASKD 600 GCDLSSLRRV GSGAAPLSKE MSLEFRKLFP WVELRAGYGL TESCGGATFF GSDKDAKAHP 660 EACGKLIPTF CAKVVDIETG KPLPPLKEGE LWLKSGTIMK EYLGNIEATT ATIDSEGWLR 720 TGDLGYIDEN GIVYIVERIK ELIKHKGYQV APAELESVLL SHPLIVDAAV IPVEDEETGQ 780 IPMAYVVRAA GSQLTEDQVI QFVAGQVAPY KKVRRVSFID GIPRSAAGKI LRKDLVLQSK 840 YQLVSKL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00693 | secretory_peroxidase | 9.0e-149 | 21 | 323 | 303 | + Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
PLN02246 | PLN02246 | 9.0e-149 | 336 | 835 | 524 | + 4-coumarate--CoA ligase | ||
cd05911 | Firefly_Luc_like | 1.0e-156 | 350 | 831 | 493 | + Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL). This family contains two functionally unique groups of proteins; one group is insect firefly luciferases and the other is plant 4-coumarate:coenzyme A ligases. However, they share significant sequence similarity in spite of their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light. 4-coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and then the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids. | ||
PLN02574 | PLN02574 | 6.0e-163 | 350 | 835 | 497 | + 4-coumarate--CoA ligase-like | ||
cd05904 | 4CL | 0 | 347 | 835 | 489 | + 4-Coumarate-CoA Ligase (4CL). 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0008152 | metabolic process |
GO:0020037 | heme 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 | AAP03021.1 | 0 | 329 | 836 | 32 | 537 | 4-coumarate-CoA ligase-like protein [Arabidopsis thaliana] |
RefSeq | XP_002271586.1 | 0 | 308 | 847 | 39 | 569 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311981.1 | 0 | 348 | 847 | 58 | 555 | acyl:coa ligase [Populus trichocarpa] |
RefSeq | XP_002315339.1 | 0 | 327 | 847 | 48 | 566 | acyl:coa ligase [Populus trichocarpa] |
RefSeq | XP_002532625.1 | 0 | 327 | 847 | 52 | 572 | AMP dependent CoA ligase, 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 | 3ni2_A | 0 | 361 | 835 | 51 | 529 | A Chain A, Structural Basis For The Recognition Of Lys48-Linked Polyubiquitin Chain By The Josephin Domain Of Ataxin-3, A Putative Deubiquitinating Enzyme |
PDB | 3a9v_A | 0 | 361 | 835 | 51 | 529 | A Chain A, Structural Basis For The Recognition Of Lys48-Linked Polyubiquitin Chain By The Josephin Domain Of Ataxin-3, A Putative Deubiquitinating Enzyme |
PDB | 3a9u_A | 0 | 361 | 835 | 51 | 529 | A Chain A, Crystal Structures And Enzymatic Mechanisms Of A Populus Tomentosa 4- Coumarate--Coa Ligase |
PDB | 3tsy_A | 0 | 351 | 835 | 80 | 576 | A Chain A, 4-Coumaroyl-Coa Ligase::stilbene Synthase Fusion Prot |
PDB | 3qya_A | 0 | 349 | 843 | 74 | 582 | A Chain A, Crystal Structure Of A Red-Emitter Mutant Of Lampyris Turkestanicus Luciferase |