CAZyme Information: OTA24376.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA24376.1
• CAZy Family: CE1|GH10
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
845	MUNK01000247|CGC1	94559.73	4.2847

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

• Gene Location: location=MUNK01000247:45382-49259(+)

Full Sequence      

MTRYYDWSVAKEKCSPDGVEIDCLLVNGEFPGPTIEANWGDIIEDLYGTSWWHSHYSSQY
ASGLVGPIVIHGPKNADYDFDLGPILVNDWYHEYYTEVTEALFAPLPEVNIPRSDNNLIN
GKNSFDCSKTSLPCEPNAPLASFNFTSGKSYRMRFINPSAAATEKITIDGHKFTVIANDF
VPIHPYETDVLTLAVGQRSDVIVEATGEPTDSVWLRAYKPQVCWPSNGGDEVKAAIFYQD
ADHSQPPTSTAGPNAYNSNCNNDPLEQTQPYYPITPGEPSSTEVIPLEFKPNNTGPSING
SHLLWYMANRTFFVNYNDPMLLETKLGNLDFPYLRNAHNYGSNSSLRFVIENTGPQPHPM
HVHGHNMFILAEGDCVSNMTVFGNEEGMSQEGNMTEYPKKRGLNVRSVEEIEKRADGQYG
SCWDGHITNPDNPQRRDVQMLAAGRYIVVQWNQDNPGVWPFHCHIAWHLSAGFVWTVVER
PDDVQKYAQIPSIMAQTFIPYGARLTNLFVKDKGGDYQDVAIGYDDGEQYLNDTLTDHTF
FGAIVGRYANRIKNSTFEIDGETSNIVANEHDGLNTLHGGEIGYDQRNWTIASHTGNSIT
FTLYDAAYQGFPGDVLNVATYTLTDEPSLISRIVSIPFNEATPIMLSNHIYWNLGAFVDE
QAVTVLNDTLYMPYADRVIDTDGILIPTGQINITNGTAYDFTKPGKQIGEDIQDAFCGTG
CQGYDTAFILDRPRYATEDPELEVLQMWAPSTGIQMSLSTNEQGLQIYSCDGQDGTTPVK
DSQQHLDDTTYLEQYGCVVIETQDWIDGINNPQWGRDQYQIFRPTSEPAINWSKYKFSVV
DPECS

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	45	473	4.4e-69	0.7625698324022346

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185696	galactose_mutarotase_like	5.18e-92	497	837	13	326	galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.
215098	PLN00194	4.21e-60	501	839	26	337	aldose 1-epimerase; Provisional
182931	galM	2.68e-57	494	840	20	342	galactose-1-epimerase; Provisional
259968	CuRO_3_MaLCC_like	4.87e-53	275	473	2	152	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. 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 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.
259947	CuRO_2_MaLCC_like	2.95e-50	82	253	1	164	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. Laccase 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO16093.1|AA1_3	3.03e-185	1	503	74	591
UJO18649.1|AA1_3	1.32e-149	1	497	155	665
USW51556.1|AA1_3	3.18e-140	1	497	135	645
QIW99529.1|AA1_3	6.79e-139	1	497	133	643
BCS07898.1|AA1_3	3.27e-138	1	497	77	582

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	3.13e-67	1	515	66	579	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.13e-67	1	515	66	579	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]
5LM8_A	1.09e-66	1	487	22	512	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.11e-66	1	487	23	513	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.02e-66	1	487	50	540	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	5.38e-122	3	497	65	565	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|D4AMB9|GALM_ARTBC	2.11e-116	482	838	57	438	Probable aldose 1-epimerase ARB_05372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05372 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	3.75e-75	1	497	72	569	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.01e-63	1	515	67	580	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q0CCX6|GEDJ_ASPTN	3.11e-63	5	494	62	575	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000001

TMHMM  Annotations     

There is no transmembrane helices in OTA24376.1.