CAZyme Information: MGYG000002372_02316

Basic Information

• Species: Clostridium_P perfringens
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P perfringens
• CAZyme ID: MGYG000002372_02316
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1215		133406.05	5.3549

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002372	3343822	Isolate	South Korea	Asia

• Gene Location: Start: 2536733; End: 2540380 Strand: -

Full Sequence      

MLKKFSNKKITALMVVLAMVFSFILPIPVKAAEISETKNSNVTEKTDKKTVNIQILATSD
LHGKFMDYDYAQGEESVGGLNQIATVVKEAKKENPNTLVLDNGDTIQGNYNHLFMNKENP
MILAMNTIGYDVFSLGNHEFNFGMDKLHNIIGQANPNLHVLCGNLYRNGERVFNPYTIKD
VDGIKVAIIGVVTPHIMQWDSQNLKGYEAKNPTEEVKKIIGEIKANGGADVYVVTSHASL
NGEYGDGDSAAGIAEANPEVSVVVAGHSHDTVKSELRGNAIISEPASRAKYVSKFNLTVE
KDESGIKVLDKNADLISLKGVQGDPELTEKLKPFHEAAINDATAKIGELKGGDLAKPDEV
KGIPQSIVEDQGITDFINEVQLYNSKKFLQTKGIDPNNVYMVSSAALFSPKANLKEGPIS
KADVSNIYKFDNKLYVIKTNGKQLKKYMEENSKFFNKYKDGDLTISFDENVRMYKYDMFE
GVNYEINIAKDPGERIENLKFSKDGKPVEDLDVVYLSVNDYRYNSGLAAGIMDPGEHEKI
YDTVNDDISAIRDLISDYIINVKHGVINRNVDGNWKIIGNNWNPEQRALAVKLINEGKIK
LPTSSNGRTPNVKSVTWDEVSKFAEALPEEKKEVEIPILTFNDFHGSLKESGGNPGAAKF
VGELKKVKEKNPNTIVVSGGDMYQGSALSNLLKGKPVSDMNKALGVQFSSVGNHEFDWGY
DLIPGWAKDGGFEFLASNIYEKATGEPVKWAKPYGVVEKGGKKIGFIGLATPETAYKTNP
DNVKDLEFRDPNTEAEKWVKHLREVEKVDAVIALTHIGSQQDRKTGEITGEVVNLTKVPG
LDAIVSAHSHMPVKGTVNGVPIVQAYKNGRAIGLIDLKFDKDGKLSVEAQRMDISKNIKD
LPVDKEMEETLGKYEKELSPILDVKVADLSEDLPHNRDAGVSPMGATVTETMRKIVDADI
AINNGGGVRAPLKKGVITVGDMYTILPFDNTIVTMDMKGSDIIKVLEHGIAPKDFGWGQH
AGLKFWYNPDAEPGNRITSVRLLDGSKLDPNKYYKLATNDFMAAGGDGYDFSAAKNIKDT
NKVLREGISDYWKNHGINPITNLATLIEPGEDKGEAVKPVEPENPSLDSNKPVEQEKPSI
DTNKPMDPTIDDINTDKHEISNPDNNSNNEENKKDDLIKLPNTGNPFGAEVFAAMGVLAT
IGGSIILKKKHNDAA

Enzyme Prediction     

No EC number prediction in MGYG000002372_02316.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	0.0	2	1100	1	1135	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	4.39e-93	626	1070	17	473	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
COG0737	UshA	4.41e-80	49	541	23	515	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	7.18e-78	629	1096	28	535	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07410	MPP_CpdB_N	1.40e-71	53	317	1	279	Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain. CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGU94268.1	4.21e-318	1	1121	1	1088
VDN48620.1	3.12e-176	33	1091	78	1112
QUI23903.1	3.66e-176	38	1098	74	1115
CDI50173.1	4.04e-165	1	616	1	601
QBD85406.1	5.02e-162	1	616	1	601

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HP1_A	2.47e-46	629	1069	2	472	5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli]
2Z1A_A	4.67e-46	636	1093	30	515	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
1HO5_A	4.27e-45	629	1069	2	481	5'-Nucleotidase(E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HO5_B 5'-Nucleotidase (E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HPU_A 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_B 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_C 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_D 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli]
1OID_A	4.83e-45	629	1069	2	481	5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OID_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OIE_A 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli]
1OI8_A	4.83e-45	629	1069	2	481	5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli],1OI8_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (P90C, L424C) [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	1.26e-106	19	1096	22	1163	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P54602	4.01e-56	622	1063	578	1037	Endonuclease YhcR OS=Bacillus subtilis (strain 168) OX=224308 GN=yhcR PE=1 SV=1
Q56878	2.64e-54	629	1095	27	533	Protein UshA OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=ushA PE=3 SV=3
P44764	5.92e-48	48	578	29	606	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=cpdB PE=3 SV=1
P08331	1.24e-47	42	577	13	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000371	0.998794	0.000239	0.000203	0.000174	0.000159

TMHMM  Annotations     

start	end
12	29