CAZyme Information: KID66526.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID66526.1
• CAZy Family: GH31
• CAZyme Description: L-ascorbate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
687	AZNF01000005|CGC1	77576.40	5.0256

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549	10891	1276135	0	10891

• Gene Location: location=AZNF01000005:1061191-1063254(+)

Full Sequence      

MSTGEDVEALEQTEEQPFLGQEAAGDKEEIEAGASPPFWLGNSRASRLHGFCKLSLFIFF
ITIILGLVSGIILSFPPRGTRDSLDTRPHDDQEKDHQDKDHTDDWKHEDISGTPRLRDTS
EYVLSPSWDRSAAPVTREYHWTVSDAELNPDGVYRSMILVNNQYPGPLIECNEFDTIIVN
VENKASNSTSIHFHGLFQNGTNWMDGTVGVTQCPIAPNSNFTYKFVVRGQSGTYWYHAHH
SAQASDGLLGPVVIHSPDELTLQEVDYATDRVIMVQDHYHNTTAELLMDYLQPDKENDEP
VPDNALINGRGVRNCDDFDGWHCDSSNASEPVFDLTAGQRHRLRFINVGAFAEFQIQIDE
HPFYITEVDGTDVHPLAFHRLNISPGQRYSVIVETNVTTADAYWLRARMVTHCFTTKNDR
LQPEIRGILRYISSSSKPLTADPQSKDWSETVETICRDLNTSALHPVQHISPPPADDFVA
LRANFMIGAWRLARGFFNESTWHANATHPSLHRFLDAKPEVTSLEAPLAINDKAFNKDND
FVLQTKGIRTVDISINNFDDGAHPFHLHGHKFFIIAQARSGYPPTSATLDKYLQQHGGMP
ENPLRRDTVTVEAYSWVIIRVVLDNPGIWALHCHNTWHSESGMVMQLLVQSEVVSEWKVD
PQHRAMCEFEGVMSGMRPDDSIWFGSF

Enzyme Prediction     

No EC number prediction in KID66526.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	153	643	1.3e-114	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.68e-71	136	643	1	517	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
215324	PLN02604	1.68e-69	136	643	24	540	oxidoreductase
259926	CuRO_1_Diphenol_Ox	2.85e-69	137	255	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
259953	CuRO_2_MCO_like_1	4.64e-67	271	431	1	162	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
259977	CuRO_3_MCO_like_4	1.58e-62	481	649	3	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI73216.1|AA1	0.0	1	687	1	687
UNI14665.1|AA1	0.0	14	687	61	758
QUC17819.1|AA1	0.0	7	687	8	713
UKZ88109.1|AA1	0.0	108	687	164	743
QGI88009.1|AA1	0.0	106	687	99	680

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.65e-71	121	648	51	541	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	4.44e-71	121	648	51	541	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
1V10_A	8.55e-65	123	645	12	485	Chain A, Laccase [Rigidoporus microporus]
5LM8_A	1.13e-63	135	648	22	503	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.16e-63	135	648	23	504	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	1.29e-96	118	667	43	578	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	1.45e-94	118	667	43	578	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	1.06e-92	118	656	43	567	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|E9R598|FETC_ASPFU	3.90e-75	131	674	17	518	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|A0A067XMP2|PTAK_PESFW	6.57e-74	135	659	63	558	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999967	0.000048

TMHMM  Annotations     

Start	End
54	76