CAZyme Information: MGYG000001458_00448

Basic Information

• Species: Cetobacterium_A somerae
• Lineage: Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Cetobacterium_A; Cetobacterium_A somerae
• CAZyme ID: MGYG000001458_00448
• CAZy Family: CBM50
• CAZyme Description: Mannosylglucosyl-3-phosphoglycerate phosphatase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
517	MGYG000001458_28|CGC1	55810.13	7.1872

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001458	3064648	Isolate	not provided	not provided

• Gene Location: Start: 1284; End: 2837 Strand: -

Full Sequence      

MNKNLKVFGLMGLVLALSACKVLPPKDGEYELTLVHVNDVHGRAKEGKYDGVGLARVATI
AKALEQDKNNGKVLLIDAGDTMHGTTFATLTKGESMVETLNAAGLDYATLGNHDFNYGQD
RLEELLSMQKYKTLAANVVDKTTGKPIAGTYDIRKIDGKKVGFFGLATPETYFKTNPNNV
KNITIADPIATAKSVVAQMKKEGVKFIVVISHLGDDESTAKNLQSVGLAEAVPEIDLIID
GHSHTELKEKKVVNGVTIVQTGEYAKNVGVVKVDFDKLKNKIEAIDYTLYTKNIIMNGDN
PVPEDAKVKATIDEISKKQEMITSVKVGESPILLEGDRAFVRTGETNLSQLITDAMLWKT
GADVALTNGGGIRASINPGEVTVGDVISVLPFGNYVITKEVKGSDLQKAVENGIRSYPES
LGAMAQVAGMTVKFNVKNPAYRRVLEIKIGNEKLNPNKTYVVATNDFMAAGGDGYSSLAG
GKELGHYPALDEVLIEYIQKVGLEGRDKVVPRLIPKK

Enzyme Prediction     

No EC number prediction in MGYG000001458_00448.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0737	UshA	4.96e-118	6	505	1	502	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	7.94e-115	23	510	652	1146	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09558	ushA	2.98e-112	1	502	1	535	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd00845	MPP_UshA_N_like	7.81e-67	32	287	1	250	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.
cd07408	MPP_SA0022_N	2.67e-62	33	286	2	255	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQY79959.1	3.51e-141	21	506	28	507
AEI45885.1	2.27e-137	32	502	49	508
AFC33532.1	4.53e-137	32	502	49	508
QZY54554.1	1.52e-136	29	502	31	492
AFK65438.1	2.43e-136	32	502	40	499

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	1.89e-69	9	510	15	531	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
1HP1_A	8.96e-58	26	500	3	498	5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli]
1OID_A	3.34e-57	26	500	3	507	5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OID_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OIE_A 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli]
1HO5_A	4.04e-57	26	500	3	507	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]
1USH_A	6.61e-57	26	500	28	532	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A9BJC1	7.73e-77	22	502	14	485	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
O34313	9.96e-71	24	513	661	1174	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
Q9KQ30	2.59e-61	13	499	15	534	5'-nucleotidase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nutA PE=3 SV=1
Q61503	1.58e-58	13	508	12	549	5'-nucleotidase OS=Mus musculus OX=10090 GN=Nt5e PE=1 SV=2
Q8DFG4	5.27e-58	17	511	19	546	5'-nucleotidase OS=Vibrio vulnificus (strain CMCP6) OX=216895 GN=nutA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000086	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001458_00448.