dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002828_00533

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Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Intestinimonas;

CAZyme ID

MGYG000002828_00533

CAZy Family

CBM50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
725	MGYG000002828_64\|CGC1	78512.69	4.3299

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002828	2102749	MAG	Singapore	Asia

Gene Location

Start: 2208; End: 4385 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002828_00533.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	2.31e-129	3	583	1	631	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	1.47e-85	13	523	2	511	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09420	cpdB	1.46e-79	14	563	1	607	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09418	PRK09418	1.96e-79	4	592	1	628	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
cd07410	MPP_CpdB_N	1.14e-70	38	305	1	277	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB41602.1	3.99e-137	35	589	34	579
BAL01252.1	1.32e-104	8	582	4	559
BBE30724.1	6.99e-101	19	597	6	620
CDI50173.1	2.45e-100	14	582	14	587
QBD85406.1	1.32e-99	14	582	14	587

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GVE_A	1.87e-37	35	335	9	340	Crystalstructure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3GVE_B Crystal structure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
4Q7F_A	1.27e-34	36	508	18	478	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	1.27e-34	36	508	18	478	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
3IVD_A	7.05e-32	36	552	5	485	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]
3JYF_A	1.11e-25	38	304	9	302	ChainA, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578],3JYF_B Chain B, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	7.94e-64	8	558	11	612	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	6.38e-47	38	563	24	605	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P53052	6.79e-47	15	555	6	600	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P26265	1.01e-45	38	563	24	605	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P44764	3.26e-44	28	563	24	615	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 help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000324	0.998881	0.000212	0.000198	0.000187	0.000164

TMHMM Annotations download full data without filtering help

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