CAZyme Information: MGYG000001477_01164

Basic Information

• Species: Clostridium_L amazonitimonense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_L; Clostridium_L amazonitimonense
• CAZyme ID: MGYG000001477_01164
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1149	MGYG000001477_7|CGC8	126718.15	5.4495

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001477	3750216	Isolate	not provided	not provided

• Gene Location: Start: 366028; End: 369477 Strand: +

Full Sequence      

MFKRLKSKRYTAFLVALVMIFSFITPMDLSAFAAEGDGVDIQVLATSDMHGRFMPYDYAT
DSEDNKGSMAQLSTMVKKLRAKNPNLVLVDNGDTIQDNSSSLFLKDEIHPMVLAMNEMGY
DAWNFGNHEFNYGVPTLKNIASKFSGAVLCGNVFDTNKEPLAKSYTIVEKGGVKIGIIGM
VTPHITKWDAENLKGYTVTNPVEEAKKSANELRGQVDIMIGLIHAGIDEEYGNGDSAREL
AKAVPDLAAVVAGHAHSTIEGEREGDVIITEPYRQANAISVIDIKVVERDGKYVIADRQK
DVKSKVVNVAPKGEEPTPVDEELVAKLKPYHDRAIEDSRTVIGELRGGDLVPKPEIKEVP
EAQIKPTAMIDLINKVQMFYGKADVSAAAVFRDDANMKEGPITKSGTTSIYKFDNTLRVL
KVNGAQLKKYMEWSAKYYNTFKPGDLTISFNESVRNYNYDMFSGVKYKIDISKENGKRIT
DLTYMDGTPVSDNDVIRLAVNDYRANTTLLNEQTGLFKGENVEVLYDSFKDMGDDGRIRD
LIRKYIVEEKGGVITPECDNNWSLTGYNWDAADRELAVKLINDGKLNIPRSADGRTPNVR
SITSKDLLMLENTVIDILSFNDFHGALKSEGKNVGAAKLAGEINRLKAINPNTIVVAAGD
LFQGSPMSNLKKGQPVAEFLKLIGLEASAVGNHEFDWGYELIPGWAKTGNFDFLATNIYD
KAAGKPVEWAKPYKVIEKGGKRIGFVGIATPETAYKTKPEIVKDFEFRDPVESINTWSKY
LRDNENVDAVIALTHLGAFQNSKTKEVTGEVADLAKNVKGVDGIITGHTHQFVSGVVNGI
PVIQGGYNGRGLANLSLVFNKEGKLSTLNSVDELYKRTDLAIDPAVKAMYDKYDKELKPI
LDEVIATLDTDLTHDRNEGLSVLGQFTTKLMAEATGSEIAVTNGGGIRTPIEKGNITMGK
MYEVFPFDNTLVTMKLKGSDLKRVIEHGIMPEGFGWGQFYGIKVYYDKDAKAGERITSMR
LLDGTPIDMDKYYKVVTNDFMHDKGDNYDLSGAIDVVDTAEPIRDAMVKIIRDMKHVSFQ
YEEHLVAGPDVTVDNNEVITPDANNKGNLPKTGSMVGSSQLLAIGSLVSLLGAFLFLNEK
HRKRNNNAA

Enzyme Prediction     

No EC number prediction in MGYG000001477_01164.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	0.0	3	1072	2	1129	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	6.43e-95	601	1049	11	473	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
COG0737	UshA	7.43e-90	14	511	3	503	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	3.49e-87	41	309	1	280	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.
PRK11907	PRK11907	2.56e-76	33	565	108	680	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGU94268.1	0.0	1	1098	1	1092
CDI50173.1	7.35e-241	1	612	1	610
AVP54978.1	1.48e-237	1	612	1	610
AAO36497.1	2.95e-237	1	612	1	610
QBD85406.1	4.17e-237	1	612	1	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D0V_A	1.60e-46	615	1048	5	484	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
5H7W_A	1.27e-45	615	1048	5	484	Crystalstructure of 5'-nucleotidase from venom of Naja atra [Naja atra],5H7W_B Crystal structure of 5'-nucleotidase from venom of Naja atra [Naja atra]
2Z1A_A	7.63e-42	635	1048	58	489	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
6VC9_A	1.87e-40	615	1050	3	484	TB19complex [Homo sapiens],6VCA_A TB38 complex [Homo sapiens],6VCA_B TB38 complex [Homo sapiens],6VCA_C TB38 complex [Homo sapiens],6VCA_D TB38 complex [Homo sapiens]
4H2I_A	3.54e-40	615	1050	4	485	Humanecto-5'-nucleotidase (CD73): crystal form III (closed) in complex with AMPCP [Homo sapiens],6TVX_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12676 (an AOPCP derivative, compound 9 in paper) in the closed state [Homo sapiens],6TW0_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12690 (an AOPCP derivative, compound 10 in publication) in the closed state [Homo sapiens],6TWA_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12646 (an AOPCP derivative, compound 20 in publication) in the closed state [Homo sapiens],6TWF_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12604 (an AOPCP derivative, compound 21 in publication) in the closed state [Homo sapiens],6YE1_A Chain A, 5'-nucleotidase [Homo sapiens],6YE1_B Chain B, 5'-nucleotidase [Homo sapiens],6YE2_A Chain A, 5'-nucleotidase [Homo sapiens],6YE2_B Chain B, 5'-nucleotidase [Homo sapiens],6Z9B_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative A830 (compound 16 in publication) in the closed form (crystal form III) [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	1.36e-108	18	1048	21	1135	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	8.01e-53	29	580	12	608	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	2.83e-51	29	572	12	603	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P54602	6.80e-51	611	1041	586	1036	Endonuclease YhcR OS=Bacillus subtilis (strain 168) OX=224308 GN=yhcR PE=1 SV=1
P44764	6.35e-50	31	581	24	630	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

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
0.000319	0.998945	0.000214	0.000197	0.000166	0.000147

TMHMM  Annotations     

start	end
12	34
1116	1138