dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002314_03968

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Basic Information help

Species

Brevibacillus_C massiliensis

Lineage

Bacteria; Firmicutes; Bacilli; Brevibacillales; Brevibacillaceae; Brevibacillus_C; Brevibacillus_C massiliensis

CAZyme ID

MGYG000002314_03968

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
621		67742.86	4.8585

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002314	4952787	Isolate	France	Europe

Gene Location

Start: 95795; End: 97660 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002314_03968.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	1.93e-134	119	620	638	1146	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	1.13e-129	138	621	15	510	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	1.07e-124	136	610	21	538	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd00845	MPP_UshA_N_like	2.70e-73	150	383	1	238	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.
cd07409	MPP_CD73_N	4.58e-69	150	383	1	263	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGA59602.1	5.43e-128	150	617	35	502
QQY79959.1	4.15e-127	144	617	33	508
QZY54554.1	5.52e-127	146	581	30	465
QUH21387.1	7.12e-122	144	618	33	508
AOT71215.1	3.02e-121	144	617	35	509

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	3.69e-87	150	617	30	528	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
5H7W_A	1.19e-71	147	618	2	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	1.22e-71	147	618	2	523	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
7QGM_A	5.72e-70	145	617	24	546	ChainA, 5'-nucleotidase [Homo sapiens]
6S7F_A	6.97e-70	150	617	4	521	HumanCD73 (5'-nucleotidase) in complex with PSB12379 (an AOPCP derivative) in the closed state [Homo sapiens],6S7H_A Human CD73 (5'-nucleotidase) in complex with PSB12489 (an AOPCP derivative) in the closed state [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	1.21e-85	150	620	669	1177	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
A9BJC1	3.88e-82	145	591	19	469	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
P29240	1.26e-74	139	618	21	547	5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1
Q05927	3.50e-71	145	617	24	546	5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E PE=1 SV=2
A0A2I4HXH5	6.52e-71	147	618	2	523	Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 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
0.001985	0.783932	0.212596	0.000862	0.000334	0.000268

TMHMM Annotations help

There is no transmembrane helices in MGYG000002314_03968.