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CAZyme Information: P175DRAFT_0517355-t39_1-p1

You are here: Home > Sequence: P175DRAFT_0517355-t39_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus ochraceoroseus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
CAZyme ID P175DRAFT_0517355-t39_1-p1
CAZy Family GT1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
741 MSFN02000005|CGC1 80562.03 4.9021
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754 9070 1392256 153 8917
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.101:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH76 2 349 1.4e-109 0.9050279329608939

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
397638 Glyco_hydro_76 0.0 1 338 13 348
Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
176257 CAD3 6.12e-145 395 739 3 341
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 1.58e-91 395 740 6 338
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism].
176207 CAD 4.49e-81 401 737 6 330
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 1.37e-65 403 738 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 741 1 751
1.21e-224 1 398 39 432
9.95e-221 1 398 39 437
4.26e-216 1 398 40 436
4.26e-216 1 398 40 436

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.16e-105 1 368 47 425
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]
9.12e-62 407 741 18 347
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]
1.26e-60 407 741 18 347
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]
1.30e-60 407 741 19 348
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]
2.30e-58 406 739 12 336
Chain A, Alcohol dehydrogenase [Moraxella sp. TAE123],4Z6K_B Chain B, Alcohol dehydrogenase [Moraxella sp. TAE123],4Z6K_C Chain C, Alcohol dehydrogenase [Moraxella sp. TAE123],4Z6K_D Chain D, Alcohol dehydrogenase [Moraxella sp. TAE123]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.50e-137 1 394 40 428
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
7.92e-131 1 394 43 433
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
5.85e-130 1 398 43 435
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DCW1 PE=1 SV=1
8.53e-124 1 394 40 434
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=DCW1 PE=1 SV=1
9.91e-121 1 398 48 444
Mannan endo-1,6-alpha-mannosidase DFG5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DFG5 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.968068 0.031943

TMHMM  Annotations      help

There is no transmembrane helices in P175DRAFT_0517355-t39_1-p1.