CAZyme Information: PV06_03534-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_03534-t43_1-p1
• CAZy Family: GH106
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
713		78181.13	5.2686

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847334.1:2096658-2100487(-)

Full Sequence      

MTVYGGHSSRTTLVSLLLVVMMMMATLSQKFSRCQVDASPSMVITTTDPGTSSSNVAAAA
AATQQQQQRDGGIPLNVSDDASIRHAASVAAYSLQSFYNGNRTGGTLGKFPYPPYYWWLS
GAAWDGMLHYWLFTGDESYNNITWMALVSQISPTNNYLPVAEMFDEGNDDIAFWAFAAMF
AAEHSFPDPPSPRYPSWLRICENVFDDFVTRWEKSSDTCGGGLRWQVFSSSAGWDYKNSI
SNGGFFQLAARLARYTGNGTYLTWAEKVWDWSERIGLVEATDLNVYDGAGIDSGLNCTKL
DHTQWSYNIAVYLYGAAVMHNITVPAGTGVRQRRGVWTNRTEGLLGVAERMFFGADDGGS
DGLKNASGVMVEQACELDWSCDVDQFSFKAYLARWMADTTVLVPHLKGRVGGLLKSSAKV
AVKACTNVDAGDARFKCGAHWYMGKWDGSIGVGQSLSVLEVVQSLLVNDTKAPENVQFIK
CDATSWDDQVVLFKLAVIVSPSKSCDVVVANAGITGPDEIFTLEDPSTEPTKPELRILNL
NLVGAMYTFKLGQHYLRARPESEDGRDRCFIFKGSVAGLLDQPGSFQYSASKFGLRGLMR
SARWTSWQEGIRVNYIAPWYTKTTILKPQVIEILASKGIEFSETADCTTAVLRIACDKSI
NGHSFAILPRSVAEHGYVDAQLDDDQGEPWNSLQKAALAASIRTMAASTQTAQ

Enzyme Prediction     

EC	3.2.1.101:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH76	82	471	5.3e-83	0.9357541899441341

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397638	Glyco_hydro_76	2.42e-134	82	459	1	348	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
187584	ADH_SDR_c_like	9.68e-32	475	675	50	243	insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs. This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
212491	SDR_c	1.49e-19	466	667	38	233	classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
395056	adh_short	6.92e-17	478	628	53	189	short chain dehydrogenase. This family contains a wide variety of dehydrogenases.
223959	FabG	4.49e-16	471	627	54	195	NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO17342.1|GH76	1.35e-118	73	474	22	402
USW51892.1|GH76	2.19e-117	73	518	20	444
SMQ49163.1|GH76	8.24e-116	72	476	18	400
SMR48979.1|GH76	8.24e-116	72	476	18	400
SMY22864.1|GH76	8.24e-116	72	476	18	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6RY0_A	5.57e-85	83	473	36	410	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]
6ZYZ_A	7.52e-11	475	639	80	231	Chain A, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_B Chain B, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_C Chain C, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_D Chain D, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZZ0_A Chain A, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_B Chain B, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_C Chain C, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_D Chain D, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZT_A Chain A, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_B Chain B, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_C Chain C, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_D Chain D, BORNEOL DEHYDROGENASE [Salvia rosmarinus],7O6Q_A Chain A, borneol dehydrogenase [Salvia rosmarinus],7O6Q_B Chain B, borneol dehydrogenase [Salvia rosmarinus],7O6Q_C Chain C, borneol dehydrogenase [Salvia rosmarinus],7O6Q_D Chain D, borneol dehydrogenase [Salvia rosmarinus]
3PGX_A	5.67e-08	506	635	107	226	Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_B Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_C Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_D Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis]
5MLN_A	6.98e-08	501	667	79	235	The crystal structure of alcohol dehydrogenase 10 from Candida magnoliae [Starmerella magnoliae],5MLN_B The crystal structure of alcohol dehydrogenase 10 from Candida magnoliae [Starmerella magnoliae]
4URE_A	7.53e-08	506	667	84	241	Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URE_B Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URF_A Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URF_B Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P36091|DCW1_YEAST	1.31e-98	73	473	22	392	Mannan endo-1,6-alpha-mannosidase DCW1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DCW1 PE=1 SV=1
sp|Q6FLP9|DCW1_CANGA	7.07e-97	72	462	18	378	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|O74556|YCZ2_SCHPO	1.27e-91	73	467	20	385	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|Q75DG6|DCW1_ASHGO	1.45e-88	75	473	24	394	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|Q5AD78|DCW1_CANAL	6.12e-87	75	473	21	395	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
0.020302	0.979660	CS pos: 28-29. Pr: 0.9409

TMHMM  Annotations     

There is no transmembrane helices in PV06_03534-t43_1-p1.