CAZyme Information: OTA37968.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA37968.1
• CAZy Family: GT22
• CAZyme Description: Peroxidase [Source:UniProtKB/TrEMBL;Acc:A0A1Z5TPP6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
594	MUNK01000015|CGC4	63347.05	5.7488

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=MUNK01000015:244723-247478(+)

Full Sequence      

MVQITSCFLALSLLFSYTQAANDTLSSCPQVWSSIASDLKRNFAGCNNLARSAVRFAFHD
SAGYSVKTPTYSPASGGADGSLLLSDEEVSRSDQNPLQGFRSFLLGKYNGYKDQDVSAAD
FVQVAGMIGVKACPGGPVVKTVVGREDNSDAAPDGLLPQAFGQRADYQTLIDLWADKGFS
PRELAALIGAHSTSRAFAQQKNGIPTGGQQDSSPRVWDVKYYSQTQSQSPPRGVYRFQSD
VNLANPETETGKAFSEFAQNPGTWAAEFSAAFYKLSIAGIPEDVAAGLTDCTAVVQAGKA
NNDQVKASNLFDCSFLTAVVTGGATGIGLMITQALVANGAKVYITSRRQEVLDNAIKLYN
TGPGSIHALPGDVSSKDGCIKLAEEMKQKEPNGIQLLVNNAGIARDDNTKFSTNGQPDMT
DPEAISQHFLKSEEKQWMDTFQTNVMGQYFMAMAFLPLLAKGREVVPGYSSSVVNVSSIS
GQMKGSSMGQFAYATSKGAFTHLSRMLGTTFAQSKVRVNVIAPGVFPSEMTTGGSNDQNK
SEMDMTSANPAGRKGHDTDMAATILMLAGRGGTFYNEQIMYPDGGNTLVQPAFK

Enzyme Prediction     

No EC number prediction in OTA37968.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	32	279	5.9e-42	0.9725490196078431

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173826	ligninase	3.05e-62	31	302	16	294	Ligninase and other manganese-dependent fungal peroxidases. Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
187646	RhlG_SDR_c	8.40e-48	310	585	1	250	RhlG and related beta-ketoacyl reductases, classical (c) SDRs. Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. 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.
223959	FabG	4.22e-40	317	587	7	251	NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].
212491	SDR_c	6.69e-39	318	583	1	234	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.
187605	Ga5DH-like_SDR_c	2.00e-34	311	585	1	245	gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs. Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO16380.1|AA2	2.83e-103	27	295	58	328
AQA29311.1|AA2	6.10e-85	28	295	48	315
UJO14060.1|AA2	6.10e-85	28	295	48	315
SMQ56086.1|AA2	9.71e-82	26	312	38	330
SMY29763.1|AA2	9.71e-82	26	312	38	330

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2B4Q_A	1.02e-29	318	585	32	273	Pseudomonas aeruginosa RhlG/NADP active-site complex [Pseudomonas aeruginosa],2B4Q_B Pseudomonas aeruginosa RhlG/NADP active-site complex [Pseudomonas aeruginosa]
2WDZ_A	1.11e-24	318	588	14	253	Chain A, SHORT-CHAIN DEHYDROGENASE/REDUCTASE [Cereibacter sphaeroides],2WDZ_B Chain B, SHORT-CHAIN DEHYDROGENASE/REDUCTASE [Cereibacter sphaeroides],2WDZ_C Chain C, SHORT-CHAIN DEHYDROGENASE/REDUCTASE [Cereibacter sphaeroides],2WDZ_D Chain D, SHORT-CHAIN DEHYDROGENASE/REDUCTASE [Cereibacter sphaeroides],2WSB_A Chain A, GALACTITOL DEHYDROGENASE [Cereibacter sphaeroides],2WSB_B Chain B, GALACTITOL DEHYDROGENASE [Cereibacter sphaeroides],2WSB_C Chain C, GALACTITOL DEHYDROGENASE [Cereibacter sphaeroides],2WSB_D Chain D, GALACTITOL DEHYDROGENASE [Cereibacter sphaeroides],3LQF_A Chain A, Galactitol dehydrogenase [Cereibacter sphaeroides],3LQF_B Chain B, Galactitol dehydrogenase [Cereibacter sphaeroides],3LQF_C Chain C, Galactitol dehydrogenase [Cereibacter sphaeroides],3LQF_D Chain D, Galactitol dehydrogenase [Cereibacter sphaeroides]
2VKA_A	9.40e-24	35	295	20	282	Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase [Pleurotus eryngii]
5FNE_A	1.19e-23	35	295	20	282	Crystal Structure Of Fungal Versatile Peroxidase From Pleurotus Eryngii Triple Mutant E37k, H39r & G330r [Pleurotus eryngii]
3FM4_A	1.60e-23	35	295	20	282	Chain A, Versatile peroxidase VPL2 [Pleurotus eryngii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A443HJZ3|VDTF1_BYSSP	1.23e-33	307	592	8	303	Short-chain dehydrogenase/reductase VdtF OS=Byssochlamys spectabilis OX=264951 GN=VdtF PE=1 SV=1
sp|Q9RPT1|RHLG_PSEAE	3.30e-29	318	585	12	253	Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=rhlG PE=1 SV=1
sp|C0KTJ6|GATDH_CERSP	5.71e-24	318	588	14	253	Galactitol 2-dehydrogenase (L-tagatose-forming) OS=Cereibacter sphaeroides OX=1063 PE=1 SV=1
sp|P50199|GNO_GLUOX	1.50e-23	309	588	5	254	Gluconate 5-dehydrogenase OS=Gluconobacter oxydans (strain 621H) OX=290633 GN=gno PE=1 SV=1
sp|A0A084B9Z1|SAT3_STACB	6.97e-23	331	589	1	266	Short-chain dehydrogenase/reductase SAT3 OS=Stachybotrys chartarum (strain CBS 109288 / IBT 7711) OX=1280523 GN=SAT3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000187	0.999786	CS pos: 20-21. Pr: 0.9798

TMHMM  Annotations     

There is no transmembrane helices in OTA37968.1.