CAZyme Information: MGYG000002357_00815

Basic Information

• Species: Bacillus licheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
• CAZyme ID: MGYG000002357_00815
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1444	MGYG000002357_1|CGC12	158162.42	5.0344

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002357	4208157	Isolate	South Korea	Asia

• Gene Location: Start: 828509; End: 832843 Strand: -

Full Sequence      

MGIQKRRFSRKNILRILLTSVMILSLLMPNTQTYAEEQNEHPLISLSILGTTDIHAHMMD
YDYYADKETAEFGLARTAQLIEKYRSRNPNTILVDNGDLIQGNPLGEYIFKHERESIISG
TKTHPIIDVMNKLQYDAGTLGNHEFNYGLEFLDGTIKGAEFPIVNANIKTPDGKNKYTPY
HIEDRTVTDESGRKHQLKVGYIGFVPPQILTWDKKHLDGKITVQDITESAKETIPKMKQE
GADVIIAIAHSGIENGEQAAGAENAVYDLALKTEGIDAIISGHQHGLFPGTDYPGNGVID
NQKGTINGIPVVMPKNWGSHLGIIDMQLELDGGKWKVKDASAKTEAIAGNVMSRNETVVS
AIKDTHEKTLEYVRAPVGQTEADINSFFAQVKDDPSIQIVTDAQKWYAEDVMKGTEYENL
PILSAGAPFKAGGRNGAGYYTNIKAGNLAIKNIGDLYLYDNTLYIVKLTGSEVKDWIEMS
AGQFNQIDPSKSGEQALLNPDFRSYNFDVIDGVTYQIDVTQPAKYNASGGVKNPQANRVK
QLSYNGKPVRDDQEFLVVTNNYRASGGGGFPHLTQDKVVYAAADENRQVLMNYIMEKKTV
NPAADNNWSIAPIKGADVTFESSLLAKPFAEKANDIDFVRESENKGYGVYKLNFDGSEPP
VDDENWTLTVMHTNDTHAHLDGAARRAAKVKEIRSETENNVLLDAGDVFSGDLYFTKWNG
LADLKLMNMMGYDAMTFGNHEFDKGPKVLADFLSGNYTAVDPLNRHQLEKPDFPIVSSNV
DVSKEPKLRSFQKEPAVLAAGKKKESGIYPYILLDVNGEQVGVFGLTTEDTSYTSSPGPN
IAFHDAYQSAEKTVKELKEKEKVNKIIALTHLGYNRDLELAKKVKGIDLIIGGHTHTLVD
HLKVVENEEPTIVAQVKDYGQFLGRVDVVFDENGVVQTDQSRFNLIAIDDKVDEDPPGKE
VLDGFKEDIDELKKKKVGYADVPLDGKREHVRSKETNLGNFIADGMLKKAKQAGGADIAI
TNGGGIRSGIAKGEITLGDVLTVMPFGNTLYAADLTGAQIKEALEHGVSQVEEGGGAFPH
VSGLSFTFTLSKPKGERILDVNLVNDKGDAVPLDLDKTYRVATNNFMGGGGDGYSVFKEA
KNGVDLGFTDYDIFTEQLALYDSVSPNIENRITEVFLPDRQADGTWTLAEKPFETYGKNA
NQAIAYFPDTEKEHIKLNMTKAQTDLVKERTGDPSITLKNDRIAMQLPAVNLASEKTKIS
IKIAKDIKQAVTKVYDFNIQQNGKTVSTFKEPVGLLFQVDAPDKHLSVYYVDRKNNSFTK
VTNGYTKGRTVAGYVDHFSEYTVMNDNDAGSPSLPPGSGDDDTPDGGSGGEPPASPGAGS
GGDGSGGHDSGGADDGNEPSDGSNGGFLPDTASNAYHWLMLGLLLLISGSGLYLYQRKRR
KLQI

Enzyme Prediction     

No EC number prediction in MGYG000002357_00815.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09418	PRK09418	0.0	9	645	4	644	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK11907	PRK11907	0.0	18	664	88	735	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09420	cpdB	0.0	44	654	24	647	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09419	PRK09419	0.0	5	1192	1	1163	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
TIGR01390	CycNucDiestase	0.0	44	654	1	624	2',3'-cyclic-nucleotide 2'-phosphodiesterase. 2',3'-cyclic-nucleotide 2'-phosphodiesterase is a bifunctional enzyme localized to the periplasm of Gram-negative bacteria. 2',3'-cyclic-nucleotide 2'-phosphodiesters are intermediates formed during the hydrolysis of RNA by the ribonuclease I, which is also found to the periplasm, and other enzymes of the RNAse T2 family. Bacteria are unable to transport 2',3'-cyclic-nucleotides into the cytoplasm. 2',3'-cyclic-nucleotide 2'-phosphodiesterase contains 2 active sites which catalyze the reactions that convert the 2',3'-cyclic-nucleotide into a 3'-nucleotide, which is then converted into nucleic acid and phosphate. Both final products can be transported into the cytoplasm. Thus, it has been suggested that 2',3'-cyclic-nucleotide 2'-phosphodiesterase has a 'scavenging' function. Experimental evidence indicates that 2',3'-cyclic-nucleotide 2'-phosphodiesterase enables Yersinia enterocolitica O:8 to grow on 2'3'-cAMP as a sole source of carbon and energy (). [Purines, pyrimidines, nucleosides, and nucleotides, Other]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLG37215.1	4.67e-230	44	656	36	665
APO43595.1	6.24e-228	44	656	34	663
QZN77538.1	1.32e-227	44	656	36	665
QOS76560.1	3.95e-227	44	656	36	665
QKS58250.1	2.24e-225	44	656	36	665

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GVE_A	3.07e-162	42	374	8	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]
2Z1A_A	2.07e-116	666	1172	28	528	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
5EQV_A	1.86e-99	44	373	8	338	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]
3JYF_A	4.05e-97	44	373	7	337	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]
4H2I_A	2.24e-77	666	1172	2	521	Humanecto-5'-nucleotidase (CD73): crystal form III (closed) in complex with AMPCP [Homo sapiens],6TVX_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12676 (an AOPCP derivative, compound 9 in paper) in the closed state [Homo sapiens],6TW0_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12690 (an AOPCP derivative, compound 10 in publication) in the closed state [Homo sapiens],6TWA_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12646 (an AOPCP derivative, compound 20 in publication) in the closed state [Homo sapiens],6TWF_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12604 (an AOPCP derivative, compound 21 in publication) in the closed state [Homo sapiens],6YE1_A Chain A, 5'-nucleotidase [Homo sapiens],6YE1_B Chain B, 5'-nucleotidase [Homo sapiens],6YE2_A Chain A, 5'-nucleotidase [Homo sapiens],6YE2_B Chain B, 5'-nucleotidase [Homo sapiens],6Z9B_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative A830 (compound 16 in publication) in the closed form (crystal form III) [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	0.0	1	1440	1	1456	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	3.94e-182	44	653	22	644	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	4.50e-180	44	623	22	611	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	1.07e-173	44	653	27	649	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764	6.07e-169	9	653	3	654	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000503	0.998534	0.000406	0.000200	0.000190	0.000160

TMHMM  Annotations     

start	end
13	35
1416	1435