dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003721_00935

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Basic Information help

Species

Peptoniphilus_C urinimassiliensis

Lineage

Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Peptoniphilus_C; Peptoniphilus_C urinimassiliensis

CAZyme ID

MGYG000003721_00935

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
760		82418.25	9.2686

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003721	1482893	MAG	Canada	North America

Gene Location

Start: 2256; End: 4538 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003721_00935.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0737	UshA	1.56e-111	15	517	5	513	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	9.18e-110	29	515	653	1143	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09558	ushA	2.48e-100	2	516	1	549	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07408	MPP_SA0022_N	5.87e-66	37	285	1	242	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	1.42e-61	37	298	1	254	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY79959.1	2.36e-152	3	529	6	526
QSX07077.1	4.38e-135	1	537	1	525
AGA59602.1	1.07e-134	14	532	15	519
AJS60070.1	1.17e-134	2	528	4	529
ABW18467.1	3.28e-134	3	547	29	572

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	2.92e-65	36	525	29	539	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
5H7W_A	1.84e-50	37	516	5	523	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]
7D0V_A	4.31e-49	37	521	5	528	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
3IVD_A	1.71e-47	35	522	5	503	Putative5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVD_B Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVE_A Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine [Escherichia coli O6]
4H2F_A	1.33e-45	37	515	26	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	4.43e-75	37	515	669	1174	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
A9BJC1	5.12e-64	3	502	2	482	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
P29240	1.52e-54	37	527	32	558	5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1
A0A2I4HXH5	1.01e-49	37	516	5	523	Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1
B6EWW8	2.46e-48	37	521	44	567	Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000328	0.998855	0.000216	0.000227	0.000192	0.000163

TMHMM Annotations download full data without filtering help

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