CAZyme Information: MGYG000002464_01879

Basic Information

• Species: Acetivibrio_A ethanolgignens
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetivibrio_A; Acetivibrio_A ethanolgignens
• CAZyme ID: MGYG000002464_01879
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
763	MGYG000002464_154|CGC1	83007.5	9.0212

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002464	3659621	Isolate	not provided	not provided

• Gene Location: Start: 12132; End: 14423 Strand: +

Full Sequence      

MRLFGKRLLTALLAASLVLPGCAPAAMAAETTGTKEIQILATSDLHGKFVPYDYALNAES
TSGSLAQVSTMIREKRNSNTILVDVGDTIESNSASLFFDEEIHPMIAGFNMLNYDFWVAG
NHEFNHGVDTLLKVADKFKGTFLCGNVYDKGTGKAIGDCYKIVEKDGVKVAVIGMVTPNI
TRWDSENLKNYKVTNPLDELKTVIEAADKEADVIVAALHMGVEGEYGVKGSGAEEIAEAF
PQIDVILAAHGHEVRNEEKNGVLIIENKNQGQTLTDVDITVKADGKGGYEVTAAKAEISS
ANGVKADEEMVKALSKYDERAKKDAVTVVGELKGGDLVPETEIPGVTQSQIEETAMINLI
NQVQMYYAKAEVSAAAAFSATANMKEGKIRKCDNALIYKYDNTLYRLEMTGKQLKQYMEW
SAKYYNTYKEGDLTVSFNENVRGYNYDMFTGVKYEVNISKEPGNRIENLTRMDGTPVKDT
DKLVVAVNNYRATSHLLTWGEVYVKENGDTLPKLLEKDVMAGETVRGLIGRWITEKNKGI
IRPVLDGNWKITGNSWNEGLHDKAAELVKAGKLTIPTSSDGRTPNVKSITIADLKDYVSV
AAVKVNANGGKASAKIFYAEEGEVYGTLPTATRKGYVFQGWYTKKDGGKKVTESSKAASG
TIYAGWTKVTAPATAQIKSVKAGKNTLTVKLDSVKGAKGYRVYYSTDKNFKKGVKSVDTS
KTSVTVKNLSSKTYYVKVKAFKADSTGAKVLGKAGNVKKATVK

Enzyme Prediction     

No EC number prediction in MGYG000002464_01879.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	3.16e-139	25	633	30	678	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	9.33e-77	23	494	13	499	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	2.29e-74	37	298	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.
PRK09418	PRK09418	1.10e-48	20	549	20	605	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
cd00845	MPP_UshA_N_like	5.46e-48	37	286	1	243	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
CDI50173.1	1.68e-220	34	604	35	615
AAO36497.1	7.70e-219	34	604	35	615
AVP54978.1	6.20e-218	34	604	35	615
QBD85406.1	9.99e-217	34	604	35	615
SNV84369.1	3.11e-207	34	598	35	609

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3JYF_A	1.78e-27	34	297	6	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]
5EQV_A	2.45e-27	31	297	4	303	1.45Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site [Yersinia pestis CO92]
3GVE_A	5.06e-26	37	303	12	315	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]
3QFK_A	1.51e-24	37	492	20	479	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
4Q7F_A	1.51e-24	37	492	20	479	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	3.67e-43	8	551	17	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	2.07e-42	28	569	15	621	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	1.25e-41	28	570	15	622	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P53052	5.86e-36	6	569	3	626	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764	6.26e-35	36	554	33	611	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

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000366	0.262163	0.736605	0.000461	0.000247	0.000148

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002464_01879.