CAZyme Information: HCAG_01819-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_01819-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320	CH476655|CGC2	34928.75	6.6786

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476655:6335169-6336418(+)

Full Sequence      

MTLGDSEPTAAVILPEHKAIVDVLAGYGVDVFELVDPSELAQSTSTSFFVPAITCRLVSE
IFPQQVFLRSTPEYTEWRNLFWSQQQSESKPACILQPTSSRQVAIALLIARLWNCPFAVK
SGGHAAFAGASSITDGLTIDLQRLNTIQLASDKKSVRVGPGNRWIDVYKSLEPQSLTAIG
GRVSDIGVGGLTLGGGISFYSAQYGFACDNVNSFEVVIANGRILNVNKQSHPDLYWALRG
GGNNFGIVTRFDLAIYSVEELWAGSQIYVVYDRTRKSLLAAVVKFADEWPFRSPGCINLQ
FCICPKACSSQPSTWNIRSS

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	82	291	5e-65	0.44541484716157204

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.57e-20	91	227	1	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
223354	GlcD	1.34e-16	78	256	19	204	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	1.51e-10	89	250	63	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	2.10e-04	82	248	7	171	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
178402	PLN02805	0.003	71	253	111	302	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	4.33e-21	66	260	40	234
QRD93627.1|AA7	5.44e-21	62	256	26	214
QMW46638.1|AA7	5.44e-21	62	256	26	214
UDD63515.1|AA7	5.44e-21	62	256	26	214
QLI74064.1|AA7	6.28e-21	69	290	43	264

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	7.56e-30	54	268	10	221	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYG_A	1.43e-29	54	268	10	221	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYF_A	1.43e-29	54	268	10	221	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
4XLO_A	2.71e-29	54	268	10	221	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
6FYE_A	2.71e-29	54	268	10	221	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	1.48e-62	79	290	67	278	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|B6H064|PRX3_PENRW	4.49e-52	52	268	29	245	FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1
sp|W6Q5R7|PRX3_PENRF	8.78e-52	52	268	29	245	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A023I4D6|PRX3_PENRO	8.78e-52	52	268	29	245	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	1.73e-45	65	284	56	275	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM  Annotations     

There is no transmembrane helices in HCAG_01819-t26_1-p1.