CAZyme Information: PHYBL_128841T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_128841T0-p1
• CAZy Family: GH15
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
271		30542.44	6.1218

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC41:316373-317463(+)

Full Sequence      

MSTENSADKYDLVRKDIIKVFPEEEYDDGSFAPVVLRLAWHASGTYDHKHKDGGSDGATM
RHNTEASDPANAGLDVARNVLEPIKQKHPWISYADLWTLGGCVAIEHMGGPHIEWTGGRR
DKHSDADCPPVGRLPDAALGKDHVLAVFVNRMGFTVQETVALIGAHTVGRCHRDRSGFDG
PWTVTPTRFSNQFFKQLLAQTWVERKWDGPRQFEDVETQELMMLPTDIALLDEPFRKYVD
IYAQDKQKFFDDFSSAFLKLIELGVAKRGKL

Enzyme Prediction     

No EC number prediction in PHYBL_128841T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA2	22	265	1.7e-63	0.9450980392156862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173825	ascorbate_peroxidase	1.78e-123	1	265	4	250	Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
178218	PLN02608	2.21e-80	32	264	31	243	L-ascorbate peroxidase
178467	PLN02879	2.91e-70	32	268	34	250	L-ascorbate peroxidase
166005	PLN02364	7.38e-66	32	264	33	246	L-ascorbate peroxidase 1
173823	plant_peroxidase_like	6.14e-58	26	262	12	255	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BDA47129.1|AA2	4.99e-106	3	265	81	346
BCS01357.1|AA2	7.52e-103	5	270	2	274
BCS13101.1|AA2	7.52e-103	5	270	2	274
QKY15243.1|AA2	8.65e-103	10	265	108	362
USW52153.1|AA2	3.51e-102	10	267	7	268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AMM_A	1.41e-73	33	264	27	258	Structure of Leishmania major peroxidase D211N mutant [Leishmania major],5AMM_B Structure of Leishmania major peroxidase D211N mutant [Leishmania major]
4GED_A	1.88e-73	33	264	27	258	Crystal Structure of the Leishmania Major Peroxidase-Cytochrome C Complex [Leishmania major]
5AL9_A	2.00e-73	33	264	27	258	Structure of Leishmania major peroxidase D211R mutant (high res) [Leishmania major],5ALA_A Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major],5ALA_B Structure of Leishmania major peroxidase D211R mutant (low res) [Leishmania major]
3RIV_A	2.06e-73	33	264	28	259	The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin],3RIV_B The Crystal Structure of Leishmania major Peroxidase [Leishmania major strain Friedlin]
3RIW_A	6.67e-72	33	264	28	259	The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin],3RIW_B The Crystal Structure of Leishmania major Peroxidase mutant C197T [Leishmania major strain Friedlin]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4PD66|CCPR2_USTMA	3.08e-106	10	265	7	268	Putative heme-binding peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CCP2 PE=3 SV=1
sp|Q6URB0|CCPR_CRYNH	3.46e-101	8	268	105	364	Cytochrome c peroxidase, mitochondrial OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CCP1 PE=3 SV=1
sp|P0CP55|CCPR_CRYNB	2.80e-100	8	268	105	364	Cytochrome c peroxidase, mitochondrial OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CCP1 PE=3 SV=1
sp|P0CP54|CCPR_CRYNJ	2.80e-100	8	268	105	364	Cytochrome c peroxidase, mitochondrial OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CCP1 PE=3 SV=1
sp|P0C0V3|CCPR_EMENI	9.62e-100	23	271	104	351	Cytochrome c peroxidase, mitochondrial OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=ccp1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_128841T0-p1.