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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 Start: 709773; End:714399  Strand: +

Full Sequence      Download help

MVPRAPSREA  LTLLKHSVRP  SVVVRSQTQR  CLLSSTTRPT  LPSHAQSQIP  QKSIRNTATF60
THSHHAEAVS  VIPTTVDTSN  ADFKENKRQM  DEATENLVNL  HTKIAQGGPQ  KARDKHIQRG120
KMLVRDRISA  LIDPGTPFLE  LSQMAGYDMY  GEDDVPAGGI  VTGIGTVNGV  QCMVVANDAT180
VKGGTYYPVT  VKKHLRAQTI  AQENRLPCIY  LVDSGGANLP  NQADVFPDVN  HFGRIFYNQA240
RMSAMGIPQI  SVVMGPCTAG  GAYVPSMSDE  NIIVENQGHI  FLAGPPLVKA  ATGEVVSAED300
LGGGKLHSEV  SGVTDYLAVD  DAHALVLARR  SVGNLNWHRN  QTVTQQPAFQ  EPLYDPQELS360
GIVGTNLRRQ  IPIHEIIARI  VDGSSFDEFK  PLYGSTLVTG  FAKIYGHPVG  IVANNGILFS420
ESSLKGAHFV  QLCGKRHIPL  IFLQNISGFM  VGQDAEKGGI  AKNGAKLVTA  VSCVDVPKFT480
VVVGSSAGAG  NYGMCGRAYS  PRLLFTWPNA  KTSVMGAEQL  SSVMEAVGKK  VDPALKARIE540
HESEATFGSA  RLWDDGIIPP  EHTRRVLGMG  LQMACGGQNK  GVEKESTWAS  IKDVSSQVAK600
QLVAQYATID  DKGIHVLGGY  PGILYPPYYW  WQAGAMFGTL  LDYWHYTGDD  QYNEMVREGL660
IHQFGEHQDL  MPSNQSKNEG  NDDQVFWAFS  MIAAAEYKLK  DPPSDQPGWL  AMTQSVFNQF720
VGRYQKEVSD  GTCGGGMRWQ  IYPWLNGWTY  KNTASNGGLF  HLGARLAMYT  KNDTYARWAE780
KAFDWMAQSP  ILPGDGQVYD  GTSITTNPPC  HDADQTPWTY  NYGIMIAGAA  YMYNYTNGAE840
KWRTELTKFI  NKVAIFFPEE  KGGVMVEICE  ANQVCDADQE  SFKAYLARWL  GITMQMAPEF900
TPQILPKLQK  SAVAAAQTCE  GPSQHNGGPH  QCGMKWYATG  FDGIGGVGPQ  MTALNVISVL960
NAQRVPPPYS  RDTGGTSEGN  PGLGSGNDDD  RLPKFQSEIT  TGDKAGAAIL  TILMFGLFAG1020
GAVWILM1027

Enzyme Prediction      help

EC 3.2.1.101:1

CAZyme Signature Domains help

Created with Snap511021542052563083594104625135646166677187708218729249757346GH76
Family Start End Evalue family coverage
GH76 584 964 5.7e-97 0.946927374301676

CDD Domains      download full data without filtering help

Created with Snap5110215420525630835941046251356461666771877082187292497538574PLN0282081583MmdA115574Carboxyl_trans590954Glyco_hydro_7692580mmdA
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

Created with Snap511021542052563083594104625135646166677187708218729249755891026CAE6998605.1|GH765861026CBY02446.1|GH765901026QRC95121.1|GH765891026QSZ36627.1|GH765901026APA11655.1|GH76
Hit ID E-Value Query Start Query End Hit Start Hit End
CAE6998605.1|GH76 2.03e-289 589 1026 39 478
CBY02446.1|GH76 1.13e-276 586 1026 40 480
QRC95121.1|GH76 3.96e-241 590 1026 53 491
QSZ36627.1|GH76 1.19e-121 589 1026 33 451
APA11655.1|GH76 3.28e-121 590 1026 33 450

PDB Hits      download full data without filtering help

Created with Snap51102154205256308359410462513564616667718770821872924975695743U9R_B915734Q0G_A725865IKL_B6189846RY0_A905731ON3_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
3U9R_B 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]
4Q0G_A 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]
5IKL_B 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]
6RY0_A 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]
1ON3_A 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

Created with Snap5110215420525630835941046251356461666771877082187292497565574sp|Q9V9A7|MCCB_DROME64574sp|Q5XIT9|MCCB_RAT64574sp|Q3ULD5|MCCB_MOUSE64584sp|Q9HCC0|MCCB_HUMAN45572sp|P34385|MCCB_CAEEL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|Q9V9A7|MCCB_DROME 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
sp|Q5XIT9|MCCB_RAT 6.57e-224 64 574 23 548
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Rattus norvegicus OX=10116 GN=Mccc2 PE=2 SV=1
sp|Q3ULD5|MCCB_MOUSE 1.86e-223 64 574 23 548
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Mus musculus OX=10090 GN=Mccc2 PE=1 SV=1
sp|Q9HCC0|MCCB_HUMAN 1.38e-214 64 584 23 555
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial OS=Homo sapiens OX=9606 GN=MCCC2 PE=1 SV=1
sp|P34385|MCCB_CAEEL 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