CAZyme Information: FGRAMPH1_01T13267-p1

Basic Information

• Species: Fusarium graminearum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum
• CAZyme ID: FGRAMPH1_01T13267-p1
• CAZy Family: GH16
• CAZyme Description: phosphoribosyl transferase domain

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1136	HG970333|CGC6	125433.16	7.1544

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FgraminearumPH-1	14145	229533	2	14143

• Gene Location: location=HG970333:5579274-5582684(-)

Full Sequence      

MATLDALRIALRQQIPSEASTKALSDIEYQHGFDLFLHHNGWGNYRDFVIPKLSQLLHSQ
FSSRKEVSVLEVGSGPKSVFGYLPNFMRQKITSYSAYEPNHLFAEKLKTWLHPTKETSPF
PSLCTSYINIEPFTQETVVHEKQQIILFCHSLYGVSSKDQVVRHALDMLSEESEEGILVV
CHRDTALFLNDLVCQRSAIFPDGTFRIANSNDTINRFASFVAGCSIQSDTMRNAIHDNWR
NVCRSLARYDNNHPDTLTFASPEVIMTFTRHSTALPELTAIVPLASKDYKVKNKEAQSHV
PAAVVRPADVGQVQRCVTWALKHRFCLTVVGGGHSGHCRWRNVVSVDMGAFNQVHIVRKT
GGSNEGHPLVVAGTGCKTGDIIQAAQSEGLTVPLGARPSVGSGLWLQGGIGHLLRPHGLA
CDAIVGAVLVSVESGQVLCVGEVPCEHQPIDAIRPNNEDDLLWSLKGAGNNFGIIISVTF
NAYPARSFLVKDWSIRLKDDEHAKYILQKFATTLARPLDRESSVDAYLYYVNTQLMLGVT
LFESMETTTGKCPLPETPESFIQVIGESDCTKTVDAVGLFDTEMYMSLMHGGHGGGKTSS
FKRCVFLKDIEHINITNILLTAIDSRPSAMCYFHLLHGGWPVQEVASDVTAFGCRDWDFA
CVVTGVWPREDDDSATARATVRWVYDVVEALLPVSQGVYGADLGPDPRDAILATKAFGPN
LRKLVKMKQIFEPHGVLTYACPLSKDMLSQKMVVLVTGEHGAGKDYCANVWAAAVKGHGY
STTVIGIGDVTKREYASQRGADSERLLGDRVYKEQHREALAAFFNQQLEHRPHLAEEHFV
ESVRSANVDVLFITGMREEAPVANLWHLVSDVRLVDIHVNASHKTRGLRRQIFTNGHSIS
RGSFNCTETLVSNYRPNFVFDNDIASDDQVKAFAKYSLFPFLGNDLRRLAGMVPSVPEFP
RPGIKFRHVLEICQQKGGYKLCASLFKQHFADDWRKVDAIVSCGVGGHISAASLVLEVNV
RSSLVHLTGKLPPPTISAEKSPSHVSSHVNGVKVEGIEMRADTLRKGARVVVIDDVLATG
NTLLSMLELINRAGINMEDISVMVVAEFPIHRGRQRLRQGGFGRVGIQSLLVFDGE

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	291	523	7.5e-40	0.462882096069869

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
235028	PRK02304	2.50e-22	955	1135	12	175	adenine phosphoribosyltransferase; Provisional
223577	Apt	1.66e-20	946	1122	5	169	Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism].
396238	FAD_binding_4	2.97e-19	301	430	1	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.
177930	PLN02293	1.62e-17	946	1117	14	173	adenine phosphoribosyltransferase
223354	GlcD	8.80e-17	272	485	3	206	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	5.22e-13	301	736	63	483
EGX49222.1|AA7|CBM1	4.83e-12	301	554	164	402
CAE7214923.1|AA7	5.99e-11	298	736	60	482
QPC60539.1|AA7	7.59e-10	256	733	16	491
QRW22693.1|AA7	1.26e-09	301	740	61	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FCH_A	2.77e-16	944	1134	2	178	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	2.84e-16	944	1134	3	179	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]
1ORE_A	2.90e-16	944	1134	4	180	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]
4X44_A	2.90e-16	944	1134	4	180	Crystal Structure of Mutant R89Q of human Adenine phosphoribosyltransferase [Homo sapiens]
4X45_A	3.95e-16	944	1117	4	168	Crystal Structure of F173G Mutant of Human APRT [Homo sapiens],4X45_B Crystal Structure of F173G Mutant of Human APRT [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q54H55|Y8969_DICDI	2.20e-27	299	733	46	437	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|A7NG77|APT_ROSCS	4.81e-18	949	1122	5	166	Adenine phosphoribosyltransferase OS=Roseiflexus castenholzii (strain DSM 13941 / HLO8) OX=383372 GN=apt PE=3 SV=1
sp|Q64427|APT_MASNA	5.89e-18	945	1134	5	180	Adenine phosphoribosyltransferase OS=Mastomys natalensis OX=10112 GN=APRT PE=3 SV=1
sp|P47957|APT_MUSSI	8.01e-18	945	1134	5	180	Adenine phosphoribosyltransferase OS=Mus spicilegus OX=10103 GN=Aprt PE=3 SV=1
sp|P47956|APT_MUSPA	8.01e-18	944	1134	4	180	Adenine phosphoribosyltransferase OS=Mus pahari OX=10093 GN=Aprt PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FGRAMPH1_01T13267-p1.