CAZyme Information: Afu3g01160-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu3g01160-T-p1
• CAZy Family: GH16
• CAZyme Description: Has domain(s) with predicted 2 iron, 2 sulfur cluster binding, cellulase activity, hydrolase activity, hydrolyzing O-glycosyl compounds, iron ion binding, oxidoreductase activity and oxidoreductase activity, more

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
674		76503.77	4.9918

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr3_A_fumigatus_Af293:275321-278940(-)

Full Sequence      

MTEYDRPFSIELPAKRQAVTMAATVASWLGYIPSLAGDKELPDEPPKALPASWYYSPEIY
QLERRAIFSKRWILVTHKLRFTKPGDFLRFEEAGFSFVLCLDREGNLNGFHNICRHRAYP
LVSEDEGNVKILSCKYHGWSYSLNGKLAKAPKFEVVPGFQKENQSLFPVHVHTDALGFIW
VNLDSSPNPVPWEEDFDGVDRQERFQRFDFTQYKFDHTWQMTGDYNWKTLADNYNECYHC
TIAHPDVARLADLSYYYTVSTPGHIQHFSRPKPDKVDEDIQNASTYYFPNACMTVSPHFF
YMMRCVPTSATSCSMEYEVYRHIEASDEDFEYIDSFFKRVLDEDKHLCNAAQKNLNAGVF
VNGQLHPDLESAPLFFQNTVRSLLKSHSDEERKINREIWPARQHSAGQATAEDVAFCLGH
YNFNMISFRQCLAIAALPLAHTALALNDISSRAQSATNLCGDNDYIILESSPWIVYNMLY
NAAQMVGTQCTNYDGMTTSDSGTKEVLWSSVTDIDYVASTNNVPKGYSFVGLTQNLETKL
SAISSIPAVYNWTRTNITEFKGNICFDFMTNDVKGDSTSSSSRELMLWLQYEGGQLPIGW
TNGPAATIDNLFGTSWTLYEDINTDTGITVSTLMPTKQFEGSFSGDLKNWLLAMADLGRF
TESTYVNVGNAGYL

Enzyme Prediction     

No EC number prediction in Afu3g01160-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH12	537	672	2e-21	0.8461538461538461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176852	RHO_alpha_C	2.92e-42	217	384	1	187	C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenase (RHO) family. RHOs, also known as aromatic ring hydroxylating dioxygenases, utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC), and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this family include the alpha subunits of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase, Stenotrophomonas maltophilia dicamba O-demethylase, Ralstonia sp. U2 salicylate-5-hydroxylase, Cycloclasticus sp. strain A5 polycyclic aromatic hydrocarbon dioxygenase, toluene 2,3-dioxygenase from Pseudomonas putida F1, dioxin dioxygenase of Sphingomonas sp. Strain RW1, plant choline monooxygenase, and the polycyclic aromatic hydrocarbon (PAH)-degrading ring-hydroxylating dioxygenase from Sphingomonas CHY-1. This group also includes the C-terminal catalytic domains of MupW, part of the mupirocin biosynthetic gene cluster in Pseudomonas fluorescens, and Pseudomonas aeruginosa GbcA (glycine betaine catabolism A). This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.
239551	Rieske_RO_Alpha_N	2.56e-40	72	189	1	117	Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.
226985	HcaE	8.08e-36	49	355	5	327	Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only].
395681	Ring_hydroxyl_A	2.97e-22	213	381	4	205	Ring hydroxylating alpha subunit (catalytic domain). This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.
176892	RHO_alpha_C_CMO-like	4.46e-19	226	385	11	175	C-terminal catalytic domain of plant choline monooxygenase (CMO) and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of plant choline monooxygenase and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and a C-terminal domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Plant choline monooxygenase catalyzes the first step in a two-step oxidation of choline to the osmoprotectant glycine betaine. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW39227.1|GH12	3.18e-136	433	672	7	246
QMW27139.1|GH12	3.18e-136	433	672	7	246
BAE64005.1|GH12	3.18e-136	433	672	7	246
QRD81492.1|GH12	3.18e-136	433	672	7	246
UDD54963.1|GH12	3.18e-136	433	672	7	246

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Y8J_A	2.34e-35	50	357	42	356	Chain A, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y8S_A Chain A, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_A Chain A, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_B Chain B, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_C Chain C, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_D Chain D, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_E Chain E, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_F Chain F, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_G Chain G, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_H Chain H, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_I Chain I, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_J Chain J, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_K Chain K, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6Y9D_L Chain L, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_A Chain A, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_B Chain B, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_C Chain C, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_D Chain D, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_E Chain E, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_F Chain F, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_G Chain G, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_H Chain H, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_I Chain I, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_J Chain J, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_K Chain K, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii],6ZGP_L Chain L, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii]
6Y9C_A	3.74e-34	50	357	42	356	Chain A, Carnitine monooxygenase oxygenase subunit [Acinetobacter baumannii]
3VCA_A	1.00e-24	48	249	20	214	Quaternary Ammonium Oxidative Demethylation: X-ray Crystallographic, Resonance Raman and UV-visible Spectroscopic Analysis of a Rieske-type Demethylase [Sinorhizobium meliloti 1021],3VCP_A The 2.2 Angstrom structure of Stc2 with proline bound in the active site [Sinorhizobium meliloti 1021],5HL4_A Acoustic injectors for drop-on-demand serial femtosecond crystallography [Sinorhizobium meliloti 1021]
4QUP_A	1.31e-24	48	249	43	237	Crystal structure of stachydrine demethylase with N-methyl proline from low X-ray dose composite datasets [Sinorhizobium meliloti 1021],4QUQ_A Crystal structure of stachydrine demethylase in complex with azide [Sinorhizobium meliloti 1021],4QUR_A Crystal Structure of stachydrine demethylase in complex with cyanide, oxygen, and N-methyl proline in a new orientation [Sinorhizobium meliloti 1021]
2B1X_A	6.24e-20	49	250	23	227	Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. [Rhodococcus sp. NCIMB 12038],2B1X_C Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. [Rhodococcus sp. NCIMB 12038],2B1X_E Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. [Rhodococcus sp. NCIMB 12038],2B24_A Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. bound to indole [Rhodococcus sp. NCIMB 12038],2B24_C Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. bound to indole [Rhodococcus sp. NCIMB 12038],2B24_E Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp. bound to indole [Rhodococcus sp. NCIMB 12038]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D0C9N6|CNTA_ACIB2	6.01e-35	50	357	22	336	Carnitine monooxygenase oxygenase subunit OS=Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) OX=575584 GN=cntA PE=1 SV=1
sp|F0KFI5|CNTA_ACICP	9.71e-34	50	357	22	336	Carnitine monooxygenase oxygenase subunit OS=Acinetobacter calcoaceticus (strain PHEA-2) OX=871585 GN=yeaW PE=1 SV=1
sp|P0ABR7|CNTA_ECOLI	2.23e-32	49	357	24	338	Carnitine monooxygenase oxygenase subunit OS=Escherichia coli (strain K12) OX=83333 GN=yeaW PE=1 SV=1
sp|P0ABR8|CNTA_ECO57	2.23e-32	49	357	24	338	Carnitine monooxygenase oxygenase subunit OS=Escherichia coli O157:H7 OX=83334 GN=yeaW PE=3 SV=1
sp|O22553|CHMO_BETVU	2.10e-26	38	364	93	425	Choline monooxygenase, chloroplastic OS=Beta vulgaris OX=161934 GN=CMO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.888191	0.111811

TMHMM  Annotations     

There is no transmembrane helices in Afu3g01160-T-p1.