CAZyme Information: HCBG_07754-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCBG_07754-t26_1-p1
• CAZy Family: GT2|GT2
• CAZyme Description: iron transport multicopper oxidase FET3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
648		72759.18	8.3706

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumG186AR	9364	447093	110	9254

• Gene Location: location=GG663376:309244-311721(-)

Full Sequence      

MERTSSRRRIRKPRDELQDPPRVSSELSRTDTTSDRTTLSRSCLASVIIFLILLVSFLGV
PKSPNIAHENQAVEQSLHSDIGQKLHPETHIHRPVTTIRLNWTVTAAYLRPDGVLKRIYV
INGHFPGPVIEARSGDRLIVDVRNGLEDEGISVHWHGLHMRDANRMDGTTGVTQCAINPG
ESFLYDFNISDSQSGTYWYHAHSGLQRADGLYGGLVIHRPTTKAIRGIQSPSTESDILKY
DYQKEILLLVGDWYHRPANDVLKWYMRAASYGNEPVPDSILINGAGRFDCAMAVPARPID
CSSENLMPHLIVDPSWSYRVRVVNTGSLAGVSLRFSQGYIRLTHVDGGLEAQQLMQSRTS
NSKSIGVVYPGQRVDFILRHPQNTRAKSSLTVELDPECFKYPNPALSSVQAFPIYSTNPN
SIKPYNPQPLYLPSNAHINLTQISSSSTLLSGLPPEAQRTYVIYTKISQMSKNQNVPFGY
FNHTSWRPQSDPPYPLVALDPRHWDKNQFAISTGSEPAWVDLVVNNLDEGAHPFHLHGHN
FFVVTLHSASRGWGSYNPFNPDQQHQQYQPTSQDLSRALLRDTVQIPQRGHAVLRFRADN
PGIWLFHCHVLWHLASGMAMVFDVMNASQAGKDQGLVNGGIKEMCRYL

Enzyme Prediction     

No EC number prediction in HCBG_07754-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	114	619	1.3e-91	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.33e-74	99	622	3	521	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259977	CuRO_3_MCO_like_4	6.57e-70	461	624	1	166	The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
177843	PLN02191	1.08e-67	101	622	27	544	L-ascorbate oxidase
215324	PLN02604	9.42e-65	99	623	26	545	oxidoreductase
225043	SufI	6.68e-56	102	625	38	449	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS75251.1|AA1	0.0	166	648	1	483
QSS54105.1|AA1	5.36e-285	266	648	1	383
QGA16928.1|AA1	4.55e-212	68	623	86	668
QKX62088.1|AA1	3.60e-210	85	634	97	662
UPX44859.1|AA1	4.58e-200	85	648	80	651

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.70e-57	101	622	7	521	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
1ZPU_A	5.91e-53	97	621	2	476	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
3V9E_A	3.52e-52	94	632	63	550	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	9.16e-52	94	632	63	550	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
5LWX_A	5.55e-44	62	619	26	527	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	1.30e-66	97	622	22	493	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	3.40e-64	97	622	24	494	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1
sp|E9R598|FETC_ASPFU	1.86e-63	97	622	22	490	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|Q6CII3|FET3_KLULA	1.33e-59	97	648	27	529	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|P14133|ASO_CUCSA	2.99e-59	101	622	42	557	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999866	0.000138

TMHMM  Annotations     

Start	End
38	60