CAZyme Information: MGYG000001451_00880

Basic Information

• Species: Paenibacillus_A antibioticophila
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila
• CAZyme ID: MGYG000001451_00880
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
702		74730.8	4.3578

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001451	5573040	Isolate	not provided	not provided

• Gene Location: Start: 975607; End: 977715 Strand: +

Full Sequence      

MHLARSSFGKLLAAALVASGLLSGAAFGTAKAAETTASAEKFELRVLHTNDTHAHLDNIA
RRVTAVNEARNDSTLLLDAGDVFSGTLYYNQFNGLADLFFMNKLNYDAMTFGNHEFDKGP
EGLVEFVKAAKFPFVSANIDFSKEPVLSAYAKQDIGAPAEAGNIYPAIIKEIQGEKVGII
GLTTPESAVLASPGENIKFADEVESARQQVEALEAQGINKIVVLSHLGYTVDQELAEAVE
GIDIIVGGHSHTQLNEAEVHHADGEPTLIVQTGEYNKYLGQLDVIFDADGVLTEWQDKLI
SLDAQNDAGEYLIKGDAESEAKLKEYAAPLEELKQTVIGKTLVDLDGERSTVRTQETNLG
DLVADGMRAKVMSIVKESDVEGYVTIQNGGGIRASIGTGDITLGHLLTTMPFGNNLSALK
MTGEEIVAALENGVSGVENGEGRFPQISGMRFYYDSTKAGDVLDAVTGAKTQAGNRIVQV
QIKQADGSYSDIDPKAYYIVATNSYMADGGDFYTSMKQAKNAGRFYELNLVDYEVFREYL
DTVGTVNVQPEGRIIDVKGASLSVEFSDISGHANAAAIEEAAAAGIINGYADGSFRPDNK
VTRVELAVMVSRALKLQASTNVTGFTDEAAIPGWALSSVAALKEAGLLEGVIADSFEPSK
QVTAGEVAKILAAVTKEQAQVGDVSATLTRGEVVSLLVQALN

Enzyme Prediction     

No EC number prediction in MGYG000001451_00880.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	3.22e-141	43	557	660	1146	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
cd07409	MPP_CD73_N	2.44e-107	44	296	1	273	CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain. CD73 is a mammalian ecto-5'-nucleotidase expressed in endothelial cells and lymphocytes that catalyzes the conversion of 5'-AMP to adenosine in the final step of a pathway that generates adenosine from ATP. This pathway also includes a CD39 nucleoside triphosphate dephosphorylase that mediates the dephosphorylation of ATP to ADP and then to 5'-AMP. These enzymes all have an N-terminal metallophosphatase domain and a C-terminal 5'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.
COG0737	UshA	1.34e-105	21	557	4	514	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	1.79e-99	8	555	5	549	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd00845	MPP_UshA_N_like	8.03e-73	44	290	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
QKV20388.1	3.85e-108	29	554	13	526
CAD6619404.1	5.97e-107	42	560	26	537
CAD6599945.1	9.55e-107	42	560	26	537
CAD6615184.1	1.18e-106	42	557	26	534
CAD6616220.1	1.65e-106	42	560	26	537

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	4.89e-119	42	554	28	528	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
7D0V_A	4.30e-76	42	555	3	523	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
5H7W_A	8.16e-76	42	560	3	528	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]
6XUQ_A	6.43e-71	36	554	14	539	HumanEcto-5'-nucleotidase (CD73) in complex with A1618 (compound 1b in publication) in the closed state in crystal form III [Homo sapiens],6Z9D_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative AB680 (compound 55 in publication) in the closed form (crystal form III) [Homo sapiens]
4H2F_A	6.93e-71	38	554	20	543	Humanecto-5'-nucleotidase (CD73): crystal form I (open) in complex with adenosine [Homo sapiens],4H2G_A Human ecto-5'-nucleotidase (CD73): crystal form II (open) in complex with adenosine [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	9.49e-123	42	557	667	1177	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P29240	1.30e-78	39	561	27	553	5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1
F8S0Z7	1.80e-75	33	555	33	562	Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2
A0A2I4HXH5	4.47e-75	42	560	3	528	Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1
B6EWW8	4.87e-75	33	555	33	562	Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 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
0.000291	0.998944	0.000205	0.000216	0.000178	0.000147

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001451_00880.