CAZyme Information: AO090001000234-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090001000234-T-p1
• CAZy Family: AA11
• CAZyme Description: Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, flavin adenine dinucleotide binding, phosphomevalonate kinase activity

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
996		107524.82	6.7464

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr2_A_oryzae_RIB40:564710-567700(-)

Full Sequence      

MYGMKPKDKFIEQALEMLVEAPQGGMVVVFHRDGTLSLNGLVCHRTACFPTGAIRVLDED
EVLDNFASFVAGFVMEDTEADKATRLEWRKVCRALGRREEAYPDHLLFSSPSVMAAFTQH
ATTLPELTAQVPLVKDKTVKNREAFHHGSASIVRPTEVQHVQQCVQWARKHEVGLTVVGG
GHSGQCLWPNVVSVDMSAFDHIHILTAGKDGGESSSASVVIAGAGCKTGDIVRKTMAAGL
TVPLGARPSVGAGLWLQGGIGHLARLYGLACDAIIGAVVVSVDSGEALCIGHVPSQHRPA
GAVRPKNEYDLLWAIKGAGSNFGIVVSITFKAYVAPVHLIRSWVIPLSDSLEARRRLSDS
DNLIASKLPRNCSADAYLYWEFGQLHLGITMFEASTTRLISDTSTPTPPPVDVDTILGLD
GKIDVVDGIGLFDAEMYMSQMHGGHGGCKTSAFKRCVFLKNIGAVNVADILTTAVGTRPT
PLCYLHLLHGGGAVSQVASGATAFGCRDWDYACVITGVWPRDQDGTEIAHAVERWVYNVA
RDLLPLSSGVYGADLGPDPRDAILAAKAFGPNRPRLARLKHCSDPHNVLAYACPLPRVSM
KQRLIILVTGDSCAGKDYCADIWVSALLAYNHKGLTARAVSISDATKREYATATGADLNR
LLSDRAYKEQHRPALTAFFQDQVRHRPRLPEEHFLNVVDSAADVDVLLITGMRDEAPVAT
FSHLVPDARLLEVRVQAGEEMRRARGGCHGSDDDSNDNKNNDNGRLNLTALDHHPDLIFH
NDTTGDKAAKAFADYYLLPFCHEDLQRLTDMVRQVPDFPRLGIEFRHVLDISQQPGGLTL
CTSLLQSHFTGDWAKVDAVACCEAGGFVYASALASQVGVPLALIREAGKLPPPTISVAKS
PSHVSLSTSNGMNEKRIEMARGLIPRGGSVVVVDDVLATGNTLCAVLQLLDEAGISSKDV
TIMVVAEFPLHRGREFLRQRGFGGVKIQSLLVFDGA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	137	337	2.2e-42	0.3951965065502183

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
398111	P-mevalo_kinase	1.14e-29	608	726	1	111	Phosphomevalonate kinase. Phosphomevalonate kinase (EC:2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate, an essential step in isoprenoid biosynthesis via the mevalonate pathway. This family represents the animal type of the enzyme. The other is the ERG8 type, found in plants and fungi, and some bacteria (see pfam00288).
235028	PRK02304	9.67e-24	803	995	1	175	adenine phosphoribosyltransferase; Provisional
223354	GlcD	1.44e-19	132	589	15	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.68e-19	152	280	4	129	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.
223577	Apt	1.43e-16	805	995	5	179	Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC87672.1|AA7	1.90e-13	150	591	71	491
QRC92907.1|AA7	1.77e-12	128	588	35	483
QPC60539.1|AA7	1.29e-11	150	336	70	238
UPK94696.1|AA7	2.18e-11	151	336	65	232
CEF79461.1|AA7|1.1.3.-	2.26e-11	150	336	70	238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FCH_A	3.78e-17	804	977	3	166	Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCH_B Crystal Structure of Human APRT wild type in complex with PRPP and Mg2+ [Homo sapiens],6FCL_A Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6FCL_B Crystal Structure of Human APRT wild type in complex with AMP [Homo sapiens],6HGP_A Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGP_B Crystal Structure of Human APRT wild type in complex with Phosphate ion. [Homo sapiens],6HGR_A Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGR_B Crystal Structure of Human APRT wild type in complex with IMP [Homo sapiens],6HGS_A Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens],6HGS_B Crystal Structure of Human APRT wild type in complex with GMP [Homo sapiens]
6FCI_A	3.87e-17	804	977	4	167	Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_B Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_C Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6FCI_D Crystal Structure of Human APRT wild type in complex with Adenine, PRPP and Mg2+ [Homo sapiens],6HGQ_A Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_B Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_C Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens],6HGQ_D Crystal Structure of Human APRT wild type in complex with Hypoxanthine, PRPP and Mg2+ [Homo sapiens]
4X44_A	3.96e-17	804	977	5	168	Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]
4X45_A	3.96e-17	804	977	5	168	Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]
1ORE_A	3.96e-17	804	977	5	168	Human Adenine Phosphoribosyltransferase [Homo sapiens],1ZN7_A Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN7_B Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P [Homo sapiens],1ZN8_A Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN8_B Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution [Homo sapiens],1ZN9_A Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens],1ZN9_B Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q54H55|Y8969_DICDI	8.24e-26	152	587	51	439	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|A7NG77|APT_ROSCS	7.36e-22	808	982	5	166	Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1
sp|P47952|APT_CRIGR	7.87e-21	804	994	5	180	Adenine phosphoribosyltransferase OS=Cricetulus griseus OX=10029 GN=APRT PE=3 SV=2
sp|Q64427|APT_MASNA	1.07e-20	804	994	5	180	Adenine phosphoribosyltransferase OS=Mastomys natalensis OX=10112 GN=APRT PE=3 SV=1
sp|P36972|APT_RAT	2.70e-20	804	994	5	180	Adenine phosphoribosyltransferase OS=Rattus norvegicus OX=10116 GN=Aprt PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AO090001000234-T-p1.