CAZyme Information: MGYG000000915_00652

Basic Information

• Species: Clostridium nigeriense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium nigeriense
• CAZyme ID: MGYG000000915_00652
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2205	MGYG000000915_2|CGC1	240447.13	4.6671

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000915	3503945	MAG	China	Asia

• Gene Location: Start: 24587; End: 31204 Strand: -

Full Sequence      

MKKLLKSKLLSLFLAFTMTLGLITIPVKEVKAEIATYIVISEVYGGGGNKDAKYKNDFIE
LYNPTEVDIDLSSWKVQYASKAGSFSDKDNTILSGVIKSKGYFLIQEAKGSTGDIDLPTP
DIAGNIAMSGTDCKVRLVDNAGNVIDLVGIGTANESEGNKSAKGMSNTQSVQRKDNDGSS
EGITNGWDTNNNEADFYAKEPTPRNSKYSIDVEVIELTSLKVEEGVTLEVGESKALKLEY
IPEDTTEKGVEYTSLTPEIVAVDATGNVTGLNEGQGTIEVKSKVKPEIKTISKVTVNKAV
DKVGPIVTDLKPANGQNIGELRRPEISVTFQDQTGVDMDSVKLSINGEDVSANITKEGET
IKYLVDKDLADGSYTVSVEVKDSIGNLTKEEWSFTVGKQEKNLYFGQLHSHTNISDGTGS
IDEAYQYASNISGVDFLAVTDHSNWFDNDTKANISDGSASTKWKTGKEAADKYNKNGDFV
AIYGYEMTWSGSTGGYGHINTFNTEGFETRSNSKMNLQAYYSALKTQSQSLSQFNHPGKT
FGDFSDFSHYDGNIDKVMNLIEVGNGEGAIRSSGYFPSYEYYTRALDKGWHVAPSNNQDN
HKGKWGNANTGRTVIEASELTRESVYDAIRNMRVYSTEDENLRISYEVNGNTMGSVLSKT
DKLDFNINVKDIDNGDNIKRISIIGDGGKVVKAIDDVNSTNKEWKFSLDKSNSSYYYVKV
EQADKDIAVTAPVWVGERENFGISTVDKDKEVIVAGETFNVETNIYNNEGSSVSNIKVEY
FKNDEENHIKSEVIESIAAGSTHISKLPYSFEKPGEYSFVVKVSATINGILKEFKSSISI
EVLGENEVSIAVIDGAHQNQYVTGDYSGKVSTLTALMSQNNIKSVINTEKITDKVLEKAS
LLILSDPQSTTNATYGLVPHKYAQDELDAIARFVQKGGNVVISSKADYKDATGEYGNATQ
GNSVLEAIGAKIRFNDDQATDDVNNGGQAFRLYFDKYNTDSPWLNGIDTSKKYSFYSGST
LILPSDKSNIDVLVRGHETTYGNDADKQSDNTQIGKGEVVGLAVETLSNGAKVFVSGATF
FSNFEMDGLDYSNYQITEKVLKELAPVPEISVSKIADVRVDKDNDNIPDRFGETVVVEGY
VTSASNAAAPGNSFFDVIYIQDETAGLTVFGVSDLNIKLGQKVRIKGKVSSYLNDAQVAI
KNESTDVKIIDENINLINPNKLSTKDSMLEEKEGLLVKVEGKVTRIEGQNIFVDDGSGEA
RVYVEGYVRSSENPGVDDEWKARIEVGDTISAIGLASEDPDGHRLRVRDSAEIVKLKAKD
IEITLFHTNDSHGRVKTDKDVIGIDVISAIKNNTINSLLLDAGDTLHGLPFATLKKGQDI
ISLMKLAGYDAMTPGNHDFNYGYERLLELAKMANEGENGFPIISANVMKGKDNLINANTI
KEVAGVKIGIFGLSTPETAYKTNPNNVKGITFADPIESARKQVKDLKEKGADVIVALAHI
GIDESSEVVSTMVADEVDGIDLIIDGHSHSTLAEGITTKNGTLIASTGDYEKNLGKVVIS
LDTNSKNIVSKKASLIAKKDTTSIKGNIVVSDKIKEIDNEQNEFLSKVIGNSKVYLQGAR
EYSRTQETNLGNLITDAMLYETGAEIAITNGGGIRDSINEGEITKGEVIKVLPFGNFIVT
KYLTGAQIKEVLEHGVKSYPAAAGQFTHVAGIKYVFDADKEAGNRIITVTIDGKSIDMSK
KYLVATNDFMAAGGDEYPHFKDAKTENEFKALDEALEGYIKNLGDIKHSVEGRIVVGKNN
LPNITANDLILAVGDNFDPLNNVTAVDLEDGDLTNKIEILENTVDTTKAGEYKVVYQVKD
SQNEVTTKEIKVIVKVRVTGVVLDKTLAELKVNESIQLKATILPAEATNREVNWASSDEK
VAKVDDNGKIVAVGVGKATITVITRDGGFTATTEITVKPEDEDNTLENIVEKIENPNGKN
EIVIKNPSNSIKVEIRDIEAIKNGEGSLDVKNGNHTISIPFNLIDSNLLKEDSVIIFEMN
VIEDLSITTGIKGVKKVFEFNLFIKNGNENIQIHDFKDGFATIKLKLSDEELKGLNKDKL
AVFYYNEVTGDFEIMETTINGNEITFKTNHFSKFIVAEKTTKPENPKPEEPKPDENKPGS
GVNNNTNLPTTGGNNPTYILLIAIVAIGVGVTLFLKKKKKDVVNK

Enzyme Prediction     

No EC number prediction in MGYG000000915_00652.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	1.67e-102	1316	1794	654	1143	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	1.42e-98	1317	1786	21	501	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558	ushA	8.34e-91	1317	1787	29	538	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07408	MPP_SA0022_N	2.90e-72	1323	1574	1	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.
cd00845	MPP_UshA_N_like	1.05e-61	1323	1576	1	253	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
QUH21387.1	1.72e-150	1322	1796	38	509
QZY54554.1	5.57e-147	1322	1795	33	503
QQY79959.1	2.15e-143	1317	1796	33	510
ABW18467.1	1.45e-140	1322	1843	59	576
AOT71215.1	1.47e-137	1323	1796	41	511

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	2.03e-63	1323	1796	30	530	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
5H7W_A	2.66e-56	1322	1801	4	529	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	1.36e-54	1322	1801	4	529	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
7JV9_A	1.67e-51	1322	1794	4	522	HumanCD73 (ecto 5'-nucleotidase) in complex with compound 12 [Homo sapiens],7JV9_B Human CD73 (ecto 5'-nucleotidase) in complex with compound 12 [Homo sapiens]
7JV8_A	1.82e-51	1322	1794	6	524	HumanCD73 (ecto 5'-nucleotidase) in complex with compound 35 [Homo sapiens],7JV8_B Human CD73 (ecto 5'-nucleotidase) in complex with compound 35 [Homo sapiens],7JV8_C Human CD73 (ecto 5'-nucleotidase) in complex with compound 35 [Homo sapiens],7JV8_D Human CD73 (ecto 5'-nucleotidase) in complex with compound 35 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	3.69e-69	1281	1794	626	1174	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
A9BJC1	2.03e-60	1323	1787	24	488	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
B6EWW8	7.47e-57	1314	1801	35	568	Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1
A0A2I4HXH5	1.46e-55	1322	1801	4	529	Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1
F8S0Z7	1.49e-55	1314	1801	35	568	Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2

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
0.000882	0.998171	0.000370	0.000219	0.000183	0.000178

TMHMM  Annotations     

start	end
9	27
2176	2195