CAZyme Information: CVK95283.1

Basic Information

• Species: Fusarium mangiferae
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae
• CAZyme ID: CVK95283.1
• CAZy Family: GH154
• CAZyme Description: Phosphomevalonate kinase [Source:UniProtKB/TrEMBL;Acc:A0A1L7TGL1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
952	FCQH01000007|CGC23	105761.58	8.5167

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FmangiferaeMRC7560	16149	N/A	345	15804

• Gene Location: location=FCQH01000007:902840-905698(-)

Full Sequence      

MATLHALKKALKKVGDEAPRKPLNDKEYDDGLSLFAEASGEQTHQEKVIIPQLSELITSL
STRDEISVLEIGPGPESVLGRLPMTLRKRITKYVALEPSFQYTQSLRRWLSPKENERPLP
SLNYSFIRPAPFIKGSCPGEKYDVILFCHGLYGLKNKKEIIRHTIEMLPEDPLDGMVITF
HRAGSLIFDSLVCHRSLSFPNRAVAIKDDDGAIDSFTRFIVGYRLTTGVLYETRQAQWRT
ICRRLAGHDDDRPGHLIFSSPEIMTAMTRHANKLPDLTALVPSLPRPYKVKSRQALYNRP
AAIVRPLEISQVQSCVRWALTNRTSLAILGGGHSDHCLWPGVVSVDMSAFNKVHVVNPPQ
DVDTECWVVAEAGCKTGDIIRETMAVGVTLPLGSRPSVGAGLWLQGGIGHLARHCGLACD
AIVGAVMVDVVSGQLLCIGYVPEQHRPPNAVRHEQDEGLLWALKGAGTNFGIVISVTFKS
YTAQVFSVRNYGQPNGHDAEKTLTTKSREVSSLYPHNISSDFYLYCEGGQIRCGMTTFLC
FLEGDISTGPTPKTIDAIELFDKEMYVSKMHAGHGGNKTSAFKRCVFLKEIANPYTMKVL
ISATRDGPTPYCYLNLVHGGKAVRYVAPEETAFGCRDWDFACVVTGIWPREYDGTHTADA
VVRWVYRVVNELLPMSKGVYGADLGPDPRDSILATKAFGPNRRRLVKLKKAFDPKNILAY
TCPLTLIGLPQKLVILVTGEHGAGKDYCAGVWSAVFKAHGYSSRVVSISEATKRKYAAAK
GADPDRLINDRLYKEQHRKSLTDFYKTQLKGESFAAEKHFIELLKEDGSDALFITGMTET
APCATLSHLVHDARLIDVRVQASKATRKLRRWGDGSKCQTPDSEEYMSADDIYLPSFTFE
NETNGDEAVMWFANQRLIPFMSKELQNLAGMVPKVPKFPRKGIDFRYVLNIA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	295	525	3.4e-40	0.4650655021834061

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.53e-18	300	429	1	130	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.
223354	GlcD	1.57e-16	298	718	30	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
398111	P-mevalo_kinase	1.86e-15	737	804	1	66	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).
404385	Methyltransf_23	5.03e-04	42	171	2	110	Methyltransferase domain. This family appears to be a methyltransferase domain.
130290	Pmev_kin_anim	7.73e-04	734	872	1	133	phosphomevalonate kinase, animal type. This enzyme is part of the mevalonate pathway, one of two alternative pathways for the biosynthesis of IPP. In an example of nonorthologous gene displacement, two different types of phosphomevalonate kinase are found. One is this type, found in animals. The other is the ERG8 type, found in plants and fungi (TIGR01219) and in Gram-positive bacteria (TIGR01220). [Central intermediary metabolism, Other]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7214923.1|AA7	3.81e-12	300	717	63	482
UPK94696.1|AA7	5.06e-12	286	717	53	482
CAP69207.1|AA7	6.34e-11	294	720	58	490
CDP32688.1|AA7	6.34e-11	294	720	58	490
QPC60539.1|AA7	6.47e-11	286	717	59	494

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	3.06e-16	298	481	37	203	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
6YJO_A	3.02e-12	286	717	59	494	Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
6Y0R_AAA	5.64e-10	300	483	61	229	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
5D79_A	2.22e-08	299	475	77	241	Structure of BBE-like #28 from Arabidopsis thaliana [Arabidopsis thaliana],5D79_B Structure of BBE-like #28 from Arabidopsis thaliana [Arabidopsis thaliana]
5K8E_A	8.32e-08	300	483	61	230	Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q54H55|Y8969_DICDI	4.91e-29	298	716	46	439	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|Q796Y5|YGAK_BACSU	1.18e-18	295	720	28	438	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|P08159|HDNO_PAENI	1.56e-15	298	481	36	202	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|G3XMD0|AZAL_ASPNA	1.17e-13	290	483	49	228	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2
sp|Q5BEJ5|AFOF_EMENI	2.81e-13	304	499	63	233	FAD-linked oxidoreductase afoF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afoF 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 CVK95283.1.