CAZyme Information: OAX84937.1

Basic Information

• Species: Emergomyces africanus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces africanus
• CAZyme ID: OAX84937.1
• CAZy Family: GT57
• CAZyme Description: CN hydrolase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1B7P7R8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
629		70664.27	7.0843

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EafricanusCBS136260	8860	N/A	91	8769

• Gene Location: location=LGUA01000039:28942-32053(-)

Full Sequence      

MHSCLQPFDDIEPGLPKRQFTLSAALRSKHVRSLAVILFIFTGCQLLWVYLHPLVHPRVH
VVVENNPGVDWSRFAYVQYTTEETYLCNSLMIFETLQRLQTKPDKILMYPDNWSTNTTQP
NAIARMLLKARDEYNVKLRPISVLKASSDKTWGASFTKLLAFNQTDYQRVLSIDSDSTIL
QSMDELFLIPSAPVAIPRAYWLQPEEYALTSALVLLEPSDFEFSRIIQAIKAKSAQQFDM
DVVNSLYKDHCLILPHRPYFLISGEFRANNHSGYLGSDNEAWEPEKVFLQTKIVHFSDWP
YPKPWLRATEPTKPAANGITIVNDHTPRKTYIMAALLKKPLKLALVQLASGADKALNLSH
ARTKVLEAAKAGASLIVLPECFNSPYGTQYFPKYAETLLPSPPSKEQSPSFHALSTLASE
AKAYIIGGSIPEFVPESKKYYNTSLVFSPAGALIATHRKTHLFDIDIPGKITFKESEVLT
GGNKITIVDLPEYGKIGLAICYDIRFPESAMIAARKGAFLLLYPGAFNLTTGPLHWSLLG
RARAMDNQVYVGLCSPARDMNATYHAWGHSLVANPRAEILAEAAETEEIVYADLEPSAIE
EIRKGIPIYEQRRFDVYPDISKGDIKFEE

Enzyme Prediction     

No EC number prediction in OAX84937.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT8	76	307	1.5e-20	0.8715953307392996

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
143596	nit	3.65e-138	346	613	5	265	Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases). This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10.
133064	GT8_GNT1	1.37e-71	74	305	1	238	GNT1 is a fungal enzyme that belongs to the GT 8 family. N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.
143607	nitrilase_5	1.56e-69	346	613	5	253	Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.
223465	YafV	5.55e-68	346	620	8	271	Predicted amidohydrolase [General function prediction only].
143587	nitrilase	3.91e-66	346	613	4	253	Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes. This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS69037.1|GT8	4.51e-144	17	310	17	310
QSS51045.1|GT8	1.28e-143	17	310	17	310
QSS63276.1|GT8	6.81e-141	17	310	17	310
QVM12485.1|GT8	5.95e-105	20	310	10	303
QKX63128.1|GT8	6.29e-101	69	309	67	308

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1F89_A	6.44e-103	336	621	6	289	Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily [Saccharomyces cerevisiae],1F89_B Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily [Saccharomyces cerevisiae]
2W1V_A	4.27e-92	342	622	5	274	Crystal structure of mouse nitrilase-2 at 1.4A resolution [Mus musculus],2W1V_B Crystal structure of mouse nitrilase-2 at 1.4A resolution [Mus musculus]
1EMS_A	5.91e-38	343	617	17	285	Crystal Structure Of The C. Elegans Nitfhit Protein [Caenorhabditis elegans],1EMS_B Crystal Structure Of The C. Elegans Nitfhit Protein [Caenorhabditis elegans]
4HG3_A	5.03e-37	335	617	34	340	Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate [Saccharomyces cerevisiae S288C],4HG3_B Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate [Saccharomyces cerevisiae S288C],4HG3_C Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate [Saccharomyces cerevisiae S288C],4HG3_D Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate [Saccharomyces cerevisiae S288C],4HG5_A Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate [Saccharomyces cerevisiae S288C],4HG5_B Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate [Saccharomyces cerevisiae S288C],4HG5_C Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate [Saccharomyces cerevisiae S288C],4HG5_D Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate [Saccharomyces cerevisiae S288C]
4H5U_A	1.17e-35	335	617	34	340	Structural insights into yeast Nit2: wild-type yeast Nit2 [Saccharomyces cerevisiae S288C],4H5U_B Structural insights into yeast Nit2: wild-type yeast Nit2 [Saccharomyces cerevisiae S288C],4H5U_C Structural insights into yeast Nit2: wild-type yeast Nit2 [Saccharomyces cerevisiae S288C],4H5U_D Structural insights into yeast Nit2: wild-type yeast Nit2 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q10166|YAUB_SCHPO	6.20e-109	342	620	45	314	Hydrolase C26A3.11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC26A3.11 PE=3 SV=1
sp|P49954|NIT3_YEAST	3.31e-102	336	621	6	289	Omega-amidase NIT3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=NIT3 PE=1 SV=1
sp|Q2T9R6|NIT2_BOVIN	6.45e-94	342	617	5	269	Omega-amidase NIT2 OS=Bos taurus OX=9913 GN=NIT2 PE=2 SV=1
sp|Q9JHW2|NIT2_MOUSE	2.19e-91	342	622	5	274	Omega-amidase NIT2 OS=Mus musculus OX=10090 GN=Nit2 PE=1 SV=1
sp|Q497B0|NIT2_RAT	1.22e-90	342	622	5	274	Omega-amidase NIT2 OS=Rattus norvegicus OX=10116 GN=Nit2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999990	0.000021

TMHMM  Annotations     

There is no transmembrane helices in OAX84937.1.