CAZyme Information: ASPVEDRAFT_65200-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_65200-t33_1-p1
• CAZy Family: GH88
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
796	KV878135|CGC11	86562.63	5.8242

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878135:177195-180153(+)

Full Sequence      

MKILWQLLLISLVPVQAIEMKLDDIASVKEACQTIAKNMVSYYTGYKPGDVPGNLPDPYY
WWEAGAMFNALIDYWAYTGDDQWNEITTQGLVHQAGNNGAFMPSNQTRTEGNDDQGFWAF
AAMSAAERNFPQPPGDGPDWLAMAQATFNTQASRWDDEHCGGGLRWQIFAWNGGYSYKNT
ISNGCFFNLAARLARYTGNQTYADWATKIFDWTQDVGFMTHDYLFYDGADSGDNCTKMDR
VQWTYNSGVYLLGAAAMYNFTDGDPRWKERTEGILKAADVFFTDKPKDVLYERACEPVDT
CKVDQRSFKGYLARWMAASTQLAPFTYDMIMPKLRASASAAAKTCAGGPRNTSCGLKWTD
QKYTKQPLDIGLEMAALDVIQSTLIHRIDAPVTREDGGISKGNPAAGSENPRQSLPDMVT
RNISVADRHSRSRLRLILLVFTFNMGSAAPVFEIPTHCKAGIIEDAGPNFKVKVAQVPVP
TPGPDDILIKLNVTGLCQSDLHYMLDDLGISMATFGVCSPGHEGAGIVVQTGANVKTFKL
GDRAGIKPIMDTCGTCPSCWSDKETYCAGVVHTGLMVPGTYQQYIVSPAHYATPIPDGIP
DEVAAPVMCKSRLQPGDWAVFPGGGGGVGIQGVQLAQAMGMRPIVVDTGEEKRALAMKMG
AEAFVDFKAVPDAAAAVVEAADGIGGHGVFVTAQAAYPTALAYLGQRVGGVVMCIGIAPA
GSMTIPVDPNLLLFKNTRIQGTLVGSRHDTTRALDFARRGKLRQICEVYPIDRLPEAVDK
LRKGLVAGRIVVDFNQ

Enzyme Prediction     

EC	3.2.1.101:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH76	20	393	2.5e-117	0.9748603351955307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397638	Glyco_hydro_76	0.0	27	377	1	348	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
176257	CAD3	8.19e-127	458	794	1	341	Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
223992	AdhP	3.35e-83	459	795	5	338	D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism].
176207	CAD	8.60e-73	463	792	3	330	Cinnamyl alcohol dehydrogenases (CAD) and related proteins. Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
176186	CAD1	5.57e-64	468	793	8	337	Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA63396.1|GH76	0.0	39	796	1	751
BCS30718.1|GH76	4.83e-308	1	438	1	438
QMS79050.1|GH76	1.45e-216	5	441	5	436
BCS10548.1|GH76	5.19e-205	4	438	5	437
BCR98100.1|GH76	5.19e-205	4	438	5	437

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RY0_A	6.74e-118	21	407	29	425	Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY1_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY2_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY5_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY6_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY7_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495]
4W6Z_A	6.43e-52	453	796	1	347	YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME [Saccharomyces cerevisiae S288C],4W6Z_B YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME [Saccharomyces cerevisiae S288C],4W6Z_C YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME [Saccharomyces cerevisiae S288C],4W6Z_D YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME [Saccharomyces cerevisiae S288C],5ENV_A YEAST ALCOHOL DEHYDROGENASE WITH BOUND COENZYME [Saccharomyces cerevisiae S288C],5ENV_B YEAST ALCOHOL DEHYDROGENASE WITH BOUND COENZYME [Saccharomyces cerevisiae S288C],7KCB_A Chain A, ADH1 isoform 1 [Saccharomyces cerevisiae],7KCB_B Chain B, ADH1 isoform 1 [Saccharomyces cerevisiae],7KCB_C Chain C, ADH1 isoform 1 [Saccharomyces cerevisiae],7KCB_D Chain D, ADH1 isoform 1 [Saccharomyces cerevisiae]
1RJW_A	2.57e-51	459	792	2	334	Crystal Structure Of Nad(+)-Dependent Alcohol Dehydrogenase From Bacillus Stearothermophilus Strain Lld-R [Geobacillus stearothermophilus],1RJW_B Crystal Structure Of Nad(+)-Dependent Alcohol Dehydrogenase From Bacillus Stearothermophilus Strain Lld-R [Geobacillus stearothermophilus],1RJW_C Crystal Structure Of Nad(+)-Dependent Alcohol Dehydrogenase From Bacillus Stearothermophilus Strain Lld-R [Geobacillus stearothermophilus],1RJW_D Crystal Structure Of Nad(+)-Dependent Alcohol Dehydrogenase From Bacillus Stearothermophilus Strain Lld-R [Geobacillus stearothermophilus]
7KC2_A	4.35e-51	453	796	1	347	Chain A, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KC2_B Chain B, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KC2_C Chain C, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KC2_D Chain D, Alcohol dehydrogenase [Saccharomyces cerevisiae]
7KCQ_A	4.47e-51	453	796	2	348	Chain A, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KCQ_B Chain B, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KCQ_C Chain C, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KCQ_D Chain D, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KJY_A Chain A, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KJY_B Chain B, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KJY_C Chain C, Alcohol dehydrogenase [Saccharomyces cerevisiae],7KJY_D Chain D, Alcohol dehydrogenase [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6FLP9|DCW1_CANGA	7.08e-132	9	420	10	419	Mannan endo-1,6-alpha-mannosidase DCW1 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=DCW1 PE=3 SV=1
sp|Q75DG6|DCW1_ASHGO	1.18e-131	16	428	20	428	Mannan endo-1,6-alpha-mannosidase DCW1 OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=DCW1 PE=3 SV=2
sp|P36091|DCW1_YEAST	2.19e-131	17	421	21	423	Mannan endo-1,6-alpha-mannosidase DCW1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DCW1 PE=1 SV=1
sp|O74556|YCZ2_SCHPO	3.60e-120	16	407	18	407	Putative mannan endo-1,6-alpha-mannosidase C970.02 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC970.02 PE=3 SV=1
sp|Q5AD78|DCW1_CANAL	7.65e-119	17	407	18	411	Mannan endo-1,6-alpha-mannosidase DCW1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=DCW1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000224	0.999742	CS pos: 17-18. Pr: 0.9818

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_65200-t33_1-p1.