CAZyme Information: ATCC64974_44920-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ATCC64974_44920-t41_1-p1
• CAZy Family: GH2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
498		54244.94	5.0177

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerN402ATCC64974	11187	N/A	0	11187

• Gene Location: location=OGUI01000007.1:512076-513833(+)

Full Sequence      

MKVSSAAVPVLSILPEASLGLGSTQLCCAALQATSLRNQVLYPTSAAYNESVASYFAVNV
QLDPTCIVQPHSTEDVSLIVSTLTQTGETQCPFAVRSGGHTTWPGAADIGQGVTIDLSMM
NSTTYHKDKGVASIQPGARWQAVYKALDPYGVTVPGGRGGPVGVGGFLIGGGNTFYTARV
GFACDNIENFEVVLASGSIVNANRTSHPDLYKALKGGSINFGVVTKYDLKTLPHDMLWGG
LVVYDNSTTARQLSAAVNFTNNIHNDPYASWIGMWEYSSTTGQNIIADALEYTKPVAFAP
AFHEFTSIPNTTDTMRFATIYNLTQELVQAAGYRDVFTTGTYKNDVKVLRKAIDLHNNNI
EKAKAHVKSDYWAMDTIIQPWPKLFAQHSVEKGGNVLGLERFDENLIQILFDYSWDDARD
DDLFIGLGQSILEEVGEYAKSIGAHNEYIYLNYADKSQNPLKGYGEENVEFISRVAKQYD
PDGVFQVQVPGGFKISQV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	487	3.5e-55	0.9694323144104804

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	6.02e-21	64	485	32	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.82e-13	64	203	1	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
178402	PLN02805	2.78e-08	57	230	130	303	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW22693.1|AA7	1.06e-25	18	486	15	477
QRD93627.1|AA7	6.82e-18	40	233	24	215
UDD63515.1|AA7	6.82e-18	40	233	24	215
QMW46638.1|AA7	2.17e-17	40	233	24	215
ANF89368.1|AA7	3.14e-15	53	231	50	227

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	3.68e-21	35	228	17	205	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYG_A	6.61e-21	35	228	17	205	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYF_A	6.61e-21	35	228	17	205	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
6FYE_A	8.86e-21	35	228	17	205	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	1.19e-20	35	228	17	205	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	4.75e-171	24	497	5	478	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	5.97e-130	20	498	37	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	3.26e-90	42	496	56	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	2.15e-72	27	498	44	527	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|A0ST43|CTB5_CERNC	2.02e-62	52	498	1	459	FAD-dependent monooxygenase CTB5 OS=Cercospora nicotianae OX=29003 GN=CTB5 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.992268	0.007766

TMHMM  Annotations     

There is no transmembrane helices in ATCC64974_44920-t41_1-p1.