CAZyme Information: OTA35924.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA35924.1
• CAZy Family: GH76
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
721	MUNK01000038|CGC1	79764.42	6.2038

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

• Gene Location: location=MUNK01000038:15246-17957(-)

Full Sequence      

MPSSTEQQSFGSLSPWSEPAWCHGIPSPYYNDSHKKLRDAIRAYVDERILPYSLDWEAKG
EAPREEAMRWAQSGFAFADVPPEYRPKNLPGPAGIPVDKLDVFHLLVSTDETSRVEGGVT
SSLSGASVIGIPPVIHHGTEQQKRQWLPGLFDWTTSFCLGITEPTGGSDVANIQTTAVKS
GDGRHYIVNGYKKWITGAPWATHMTTAVRTGGAGMGGLSVLVIPMNSPGLTWRRIPNSGQ
NAGGASLVELDDVQVPVENRVGKEGDGFRIIMVNFNRERYIMAVGSNRKARTCLNIAFDY
ANKRETFGKPLISNQIIAAKFATLARYIESHWAWLESIAYAVQQSPRGWQDPDIAGRIAL
AKVQAGRIQEMAIREAQQVLGGAGYQRGGPGAPVEQQSRDLRMMVVGGGSEEIISDLAFA
GAYAASSGDSYTDVGFKITTGPYPNPSNYEGNPDPPGKSSAYALNWAQDISAEYNKSLIY
LYDFAHSGDIVNSSLISPHQSVNNTFTAQADNQFLAYLTGEDRIVNWHSSDSLFTVFFGI
NDIDRALGGDYPFLTDWDERLPLIQDSYWAHVEKLYNAGARNFAFLNLPTYWLSPGIINR
GNATVVDVARHRNLLWNHELAKRFEHFQCTHRSTFAKLVDVYGLWESMYAYPAAYGLSNV
TEYCDAYYGGTGTDLTAYNSSCSAPVNEYLWINWLHPTWTVHRYLAKLVLEAMGYLPARH
T

Enzyme Prediction     

No EC number prediction in OTA35924.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE16	428	707	2e-47	0.9700374531835206

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173849	LCAD	3.34e-76	34	418	3	367	Long chain acyl-CoA dehydrogenase. LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
224871	CaiA	1.31e-73	30	413	5	377	Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism].
173838	ACAD	1.10e-68	32	414	1	321	Acyl-CoA dehydrogenase. Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
173847	SCAD_SBCAD	7.22e-59	32	413	1	362	Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
173851	IBD	9.49e-52	31	414	2	364	Isobutyryl-CoA dehydrogenase. Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATZ46260.1|CE16	2.85e-45	423	713	46	334
EGX53944.1|CE16	4.97e-43	428	713	45	331
CBY01773.1|CE16	6.27e-42	428	717	43	329
APA06788.1|CE16	1.51e-41	423	713	46	334
QRC99106.1|CE16	3.88e-39	414	714	11	322

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3R7K_A	1.92e-54	26	417	25	396	Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196 [Mycobacteroides abscessus ATCC 19977],3R7K_B Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196 [Mycobacteroides abscessus ATCC 19977],3R7K_C Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196 [Mycobacteroides abscessus ATCC 19977],3R7K_D Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196 [Mycobacteroides abscessus ATCC 19977]
3OIB_A	1.68e-51	24	418	20	395	Crystal structure of a putative ACYL-COA Dehydrogenase from mycobacterium smegmatis, Iodide soak [Mycolicibacterium smegmatis MC2 155],3OIB_B Crystal structure of a putative ACYL-COA Dehydrogenase from mycobacterium smegmatis, Iodide soak [Mycolicibacterium smegmatis MC2 155],3P4T_A Crystal structure of a putative acyl-CoA dehydrogenase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3P4T_B Crystal structure of a putative acyl-CoA dehydrogenase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155]
4U83_A	9.78e-43	32	413	12	373	Structure of Brucella Abortus Butyryl-CoA dehydrogenase [Brucella abortus A13334],4U83_B Structure of Brucella Abortus Butyryl-CoA dehydrogenase [Brucella abortus A13334],4U83_C Structure of Brucella Abortus Butyryl-CoA dehydrogenase [Brucella abortus A13334],4U83_D Structure of Brucella Abortus Butyryl-CoA dehydrogenase [Brucella abortus A13334]
1UKW_A	6.02e-42	32	413	7	367	Crystal structure of medium-chain acyl-CoA dehydrogenase from Thermus thermophilus HB8 [Thermus thermophilus],1UKW_B Crystal structure of medium-chain acyl-CoA dehydrogenase from Thermus thermophilus HB8 [Thermus thermophilus]
2PG0_A	1.56e-40	29	417	9	378	Crystal structure of acyl-CoA dehydrogenase from Geobacillus kaustophilus [Geobacillus kaustophilus HTA426],2PG0_B Crystal structure of acyl-CoA dehydrogenase from Geobacillus kaustophilus [Geobacillus kaustophilus HTA426]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q50LG2|AF101_ALTAL	7.31e-98	10	418	5	417	Acyl-CoA dehydrogenase AFT10-1 OS=Alternaria alternata OX=5599 GN=AFT10-1 PE=3 SV=1
sp|Q5ATG5|APDG_EMENI	1.73e-97	12	418	5	418	Acyl-CoA dehydrogenase apdG OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=apdG PE=2 SV=1
sp|P45857|ACDB_BACSU	1.40e-37	37	413	10	366	Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) OX=224308 GN=mmgC PE=1 SV=3
sp|C3UVB0|ACD_DESML	8.04e-37	37	385	12	347	Glutaryl-CoA dehydrogenase OS=Desulfococcus multivorans OX=897 GN=Acd PE=1 SV=1
sp|O34421|ACDC_BACSU	1.24e-36	37	413	12	369	Probable acyl-CoA dehydrogenase YngJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yngJ PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000001

TMHMM  Annotations     

There is no transmembrane helices in OTA35924.1.