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CAZyme Information: OAG16706.1

You are here: Home > Sequence: OAG16706.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG16706.1
CAZy Family CE12
CAZyme Description 3-methylcrotonyl-CoA carboxylase 2 [Source:UniProtKB/TrEMBL;Acc:A0A177DB44]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1027 KV441489|CGC5 111672.63 6.6547
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.101:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH76 584 964 5.7e-97 0.946927374301676

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
178415 PLN02820 0.0 38 574 7 554
3-methylcrotonyl-CoA carboxylase, beta chain
227136 MmdA 0.0 81 583 2 514
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism].
395825 Carboxyl_trans 1.07e-165 115 574 1 476
Carboxyl transferase domain. All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
397638 Glyco_hydro_76 3.25e-157 590 954 1 348
Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
130187 mmdA 1.66e-80 92 580 1 501
methylmalonyl-CoA decarboxylase alpha subunit. This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.03e-289 589 1026 39 478
1.13e-276 586 1026 40 480
3.96e-241 590 1026 53 491
1.19e-121 589 1026 33 451
3.28e-121 590 1026 33 450

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.48e-206 69 574 21 540
Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC), beta subunit [Pseudomonas aeruginosa],3U9S_B Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9S_D Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9S_F Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9S_H Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9S_J Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9S_L Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, CoA complex [Pseudomonas aeruginosa],3U9T_B Crystal structure of P. aeruginosa 3-methylcrotonyl-CoA carboxylase (MCC) 750 kD holoenzyme, free enzyme [Pseudomonas aeruginosa]
1.34e-196 91 573 14 513
Chain A, Probable acetyl-/propionyl-CoA carboxylase (Beta subunit) AccD1 [Mycobacterium tuberculosis],4Q0G_B Chain B, Probable acetyl-/propionyl-CoA carboxylase (Beta subunit) AccD1 [Mycobacterium tuberculosis],4Q0G_C Chain C, Probable acetyl-/propionyl-CoA carboxylase (Beta subunit) AccD1 [Mycobacterium tuberculosis]
2.15e-142 72 586 3 531
Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit [Pseudomonas aeruginosa PAO1],5IKL_D Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit [Pseudomonas aeruginosa PAO1],5IKL_F Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit [Pseudomonas aeruginosa PAO1]
3.59e-88 618 984 57 425
Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY1_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY2_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY5_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY6_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY7_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495]
9.81e-73 90 573 12 505
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON3_B Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON3_C Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON3_D Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON3_E Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON3_F Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) [Propionibacterium freudenreichii],1ON9_A Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii],1ON9_B Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii],1ON9_C Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii],1ON9_D Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii],1ON9_E Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii],1ON9_F Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound) [Propionibacterium freudenreichii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.23e-225 65 574 23 563
Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Drosophila melanogaster OX=7227 GN=Mccc2 PE=2 SV=1
6.57e-224 64 574 23 548
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Rattus norvegicus OX=10116 GN=Mccc2 PE=2 SV=1
1.86e-223 64 574 23 548
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Mus musculus OX=10090 GN=Mccc2 PE=1 SV=1
1.38e-214 64 584 23 555
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Homo sapiens OX=9606 GN=MCCC2 PE=1 SV=1
4.74e-211 45 572 43 591
Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Caenorhabditis elegans OX=6239 GN=F02A9.10 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000057 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
1005 1026