CAZyme Information: CAH01122.1

Basic Information

• Species: Kluyveromyces lactis
• Lineage: Ascomycota; Saccharomycetes; ; Saccharomycetaceae; Kluyveromyces; Kluyveromyces lactis
• CAZyme ID: CAH01122.1
• CAZy Family: GT15
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
612	CR382123|CGC10	68932.25	5.8543

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KlactisNRRLY-1140	5389	284590	313	5076

• Gene Location: location=CR382123:133089-134927(+)

Full Sequence      

MLIEALWIVLLFGVSQCKDLKFDISRHEDGRTIRLNENDDLIKPPLRLRNGEQLNLQIEN
HLDQPTAIHFHGLLLENFVGEELATGKQPAVLGDGVPGISQYEVGVNRSYWQNITVSKTT
CGTFWYHSHYAVQYGEGLRGPVIVDCDQFDNHERDVAKEFGLGAHVQEQIITLSDWYKYP
HDFIMDAFLQPNKGADPHVDGSLFNGKQDENQVIQVDPDTEYLRLRILNMANSNTQVFHI
ANHKMIVIETDGILVKPVELSTLTLATGQRYTVLVKRDENNQNARIIHGCNKMMGYITKS
HVLQYYPSFSTAVSSSSVSISRLPDFTSIELYKKYEPIDWMLLPDPESNDQKFSLDYEQS
TSAATKQKYHTSMFFVNGDTMGEFMNPASAVPLLISMENATKKPINVGFGGTVDIAINSI
DHMRHPWHLHGHHFQVISIGESGDGPLHWDNPSSRAYAKYSEDLTYWKSSGRVPMTRDTI
NIAGSSFAVIRFQADSPGLWLLHCHVDWHMVKGLGVVIQEGLETLPLDSLVIREPTNIVT
PKPKLNPDIELLHEESISSTPTPPPTPLPTVQADADHAINTQPETSKLKVIGIYCAVVVF
LDIMLYKYMLSR

Enzyme Prediction     

No EC number prediction in CAH01122.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	514	8.4e-82	0.9553072625698324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259932	CuRO_1_MCO_like_2	9.33e-64	4	146	1	139	The second 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
225043	SufI	3.35e-61	44	518	64	446	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].
259945	CuRO_2_Fet3p_like	1.00e-50	167	307	1	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
259966	CuRO_3_Fet3p	1.85e-35	374	520	12	158	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. 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.
274555	ascorbase	5.40e-34	30	523	31	526	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEU60257.1|AA1	0.0	1	612	1	607
BAP69267.1|AA1	2.20e-265	10	607	17	635
BAO37697.1|AA1	3.90e-265	10	607	17	651
QGN14130.1|AA1	1.81e-263	10	535	17	572
AMD19517.1|AA1	1.28e-173	6	555	14	565

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.48e-47	26	520	14	479	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]
1V10_A	1.00e-40	61	531	77	500	Chain A, Laccase [Rigidoporus microporus]
1HFU_A	2.16e-36	44	522	34	470	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.18e-36	44	522	34	470	Chain A, Laccase [Coprinopsis cinerea]
3SQR_A	4.82e-34	51	525	105	547	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q04399|GMC1_YEAST	4.78e-139	6	548	14	571	Putative multicopper oxidase GMC1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GMC1 PE=1 SV=1
sp|Q09920|FIO1_SCHPO	4.37e-49	45	526	59	503	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|K7NCS2|FETC_EPIFE	6.00e-49	44	540	54	521	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	1.38e-48	24	528	32	496	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|P78591|FET3_CANAX	5.64e-48	38	538	49	516	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000212	0.999754	CS pos: 17-18. Pr: 0.9761

TMHMM  Annotations     

There is no transmembrane helices in CAH01122.1.