CAZyme Information: MGYG000001404_04330

Basic Information

• Species: Paenibacillus_L senegalensis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_L; Paenibacillus_L senegalensis
• CAZyme ID: MGYG000001404_04330
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
621		66230.89	4.2104

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001404	5495033	Isolate	not provided	not provided

• Gene Location: Start: 341559; End: 343424 Strand: -

Full Sequence      

MMKQWKNGMTAVLAALLLISVWGNGAGIASAEEVSASSDQTITIVHTNDIHSRVEESDSQ
IGYAKLSTIIKQMREANPNTVVLDAGDTFHGQTIANLVRGESIVRLLNEVGYDAMAPGNH
DFNFGSDRLQELAGLAEFPVLAANVYRTDGTRLLEPYIFVNVGDARIAIFGLATPETVYK
THPDNVSGLTFANPVEEARKVVGELEGQADIVIALAHLGLDESSEDTSRKLAQEVGGIDV
IIDGHSHTTLENGLTVGDTLIAQTGEYSYNVGVVEIALADGEVVSKQASLMTRAEVENVE
PDHNVLSIIEEVKTSQEEVLSEVIGSTAVFLDGERENVRTGETNLGNLITDAMLDETGAD
IALTNGGGIRASIAAGDITKGDVITVLPFGNYIQTKKVTGAELVEALEHGVGSYPDSLGA
FPHVSGMTFKIDENQPKGSRVHSAIIQGQPLDLNQTYLLATNDFLAAGGDDYTAFQPQPL
EGDFSSLEESVIRYVQSKGTVDVKSEGRITVAAKPGALTPPVSETPAPTPTPPATETPEQ
PEAPAQPEPTEEAWAPVQPEPPVQPETGGESGNAAQVYVVQSGDNLSKIARMFNTTWQTL
QRLNHLHNPHLIFPGQQIVLP

Enzyme Prediction     

No EC number prediction in MGYG000001404_04330.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	3.42e-125	41	515	660	1149	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	6.76e-121	16	515	1	517	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	4.36e-120	1	503	1	539	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07408	MPP_SA0022_N	7.47e-81	42	283	1	246	Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain. SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor domain. 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.
cd00845	MPP_UshA_N_like	1.38e-75	42	282	1	242	Escherichia coli UshA-like family, N-terminal metallophosphatase domain. This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. 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
AGA59602.1	7.37e-244	12	621	10	601
AEI45885.1	4.78e-215	24	621	31	592
AFH65854.2	8.33e-215	24	621	31	598
AFC33532.1	2.73e-214	24	621	31	592
AFK65438.1	2.29e-212	24	621	22	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	6.81e-75	27	515	15	534	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
1HP1_A	3.96e-62	42	503	9	504	5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli]
1USH_A	1.14e-60	28	503	18	538	5'-NucleotidaseFrom E. Coli [Escherichia coli K-12],2USH_A 5'-Nucleotidase From E. Coli [Escherichia coli K-12],2USH_B 5'-Nucleotidase From E. Coli [Escherichia coli K-12]
1HO5_A	3.47e-60	42	503	9	513	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]
1OI8_A	1.08e-59	42	503	9	513	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
A9BJC1	7.13e-88	42	509	24	496	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
O34313	2.10e-73	42	509	669	1174	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
Q9KQ30	9.25e-61	11	503	9	541	5'-nucleotidase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nutA PE=3 SV=1
P07024	6.22e-60	28	503	18	538	Protein UshA OS=Escherichia coli (strain K12) OX=83333 GN=ushA PE=1 SV=2
P29240	7.70e-60	42	509	32	546	5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 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
0.000557	0.998557	0.000224	0.000255	0.000209	0.000186

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001404_04330.