CAZyme Information: MGYG000004725_01413

Basic Information

• Species: UBA9475 sp900554075
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA9475; UBA9475 sp900554075
• CAZyme ID: MGYG000004725_01413
• CAZy Family: CE8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2464	MGYG000004725_12|CGC1	259599.46	4.2731

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004725	2206830	MAG	Denmark	Europe

• Gene Location: Start: 63575; End: 70969 Strand: -

Full Sequence      

MHKKQINRLLAAVLSIMMILSLVVIPAGAARPMGGETVAETPAGEDAGAHLSAVSRPAVN
TEPAAELFAGATEVDVWDFGAEQLANTAEYTFNNHLNVEVINSWYEGMVDKDGNPVTVKT
GQAGNNFPSTGMPNTAGLSYSTAGAFNHRLRTDNTALTRDSGDTSTGDGKDPYVAADATY
KGLLYSNSAANPAVHFALECQAGDTVTVIVASNGTDSLIQFSKAGAPAANPEDPAEPDVV
EASDVFTRASRTKAQTMVFHAKETGTYKINSVNEKLVVDRIYREHAVDVAVSGKVTEADG
MPTGYSLVFTNTTTGAETAMAVSQGAYSGTLKAPYSYDVSLKDANGFAVLVGNEVTVTKA
SASVKHNVITQGVDRVTVSGAITGLGDKATAQKLEGNLLFTPTGDGIVYIPAVTVTVADD
GSCTYSVEVEKDMPVSISAKKLNDWEITTQNITDRAFTEDTTLDLVFAKKALWPVTITTT
GMTATDLAGTKFTFTNLHEAGETEDQVAVPFNPYSDSNLTGSIYNYAYTFTGTTGVELRD
GVYDVTVDDPHQKATANLVVNGAAATLTIPFKTPAPYVSNGVHDFTPNGVTLAMVDGISG
DPTQFKPHNSGHGLAGKGDITISLAELSNITISGCCYSQVGGTLLVPTATAGGQDVTVEV
VKEGVANSEDPEYAIKGVEGDVVITFPATGTSYIHKITVEAAVMPTIAADDYKFGAFEGY
AQGDAVTSPVDGLAFGGSAKWWNTSDGMKFDNGTMTVNMKEKGTITVTGCQWSSDKTLAS
VTSDVGTVTLDESGSDPVYTIANAEGLVTITLPNNNTYIHGIKVEYPTVTYYGTDWDFRN
DGVGQGTAYYPANDAEGKVFADKNGLGELAVKGGKFQGHDTTYGTAGNGYTMTVPVMTAC
TVKVAVGYNWWVWADGTNVTSDFTEETPATHENTGTNNENGFVTFTYTGTDPGEVVIHVP
AARAATETLTKIGDSYIARVLVEYDSSVELPEPPKTDDIVYHVGASRTADGVTEFTTITD
ALTAAEQAKRAVGQRITIEIDPGNYEEQLYIKVKDLTLKNAKADQATLELKNKGVDIGDN
EVRITWYYGHGYNYYSMTNGHRYNADVMAANQANGYPSYKNAGAGSTDDSYWNASVLLAA
DNFQAEGIIFENSFNQYVSAKSVLDTIEPQGAQAKEGNVARASMKTVGDTKVQEKAYVER
AGALSIKSGSNIFFNKCAFISRQDTFYGAEGSKVACYDCDIYGGTDYIYGGMTLVAAKCD
LLFNTSEDNNDVGYITAAQQKSQRGYLMWNCTVDSTTPGVNTASAYRSKPGYFGRPWEST
TGEAVFYATDIKATDPVYFGVPLDKQTDSSTSLICPVGWNNSLGGESAKSAELGSVEFYD
DVNNTAKRVSWATVPSQAPTVADFLGDWDPFTENSLDMTISNQTPTAAPAATKPVTAIKI
TTTPKDLGVGEKLQLAATVTPSDATDPSLDWTSSDLSVATVSETGEVTAVAGGVVDITAS
SKNHMVNDHIRLTVIVPVSGVTLNKTTINMGAGRTTTLTATVAPDNATNKDVTWKSSDEK
VVTVDATGKVKGVNEGTATITVTTVDGEKTAQCAVTIVGTVPTTPDEPIDPNGAIVILHS
NDVHGAIEGYAKMAQLKADYEAKGATVLVMDAGDFSQGTTYVSVSQGETAIELMNLVGYD
VATTGNHEFDYGADNLNTLDTKADFDILAGNIMKNGQNAYTKSVMLTAGDKKIGVFGLET
PETATKAHPAKIKGLTFLAGQEMYGAAKAMVAELKADGADYIICLGHLGIDAQSEPNRSI
DLLDATVGNVTGIDVFIDGHSHSTLDDIVAVTNADRTVNGAQLTSTGTKFANIGVVTIAP
DGTITTECVATDDITVDETNAAVKAVADKAAAIKAEVDADYGAKFATSTVDLNGDRAPGN
RTEETNLGDLITDAMLWLATKDDLGVPTENVIALTNGGGIRAPIAKGDVTKNDVNTVLPF
GNTVAVDYVKGSVLLEALEASTAVTPTAMGGFPQVAGITFTVDTTKAFVADGQYPGTTVD
KPASINRVTITSINGKAFDPDAEYAVVTNDFVAAGGDSYYALSVSEKITDTGVALDEALM
EYITTVLKGTIGSDYAEPQGRITVITAENVADLLTDAIAEAEALAAETETSEDGSDVRKT
ELWVTPEAMEAYNEVIKAAKDVAASETATAEDKIEMINTLNEATAAFKALQQEGTKKTTG
GSGIGTGTKPNTTITEKRTNDNGDVTTITTQPSGDKTITVVNKDGETVAEIKLPASISAP
AVKFKDVPDDHWAAKSINDMAGLGMVKGVNEANDVFDMTSSMTRGAVATMFFRLSDGKTG
LESTFADVQGHWAADAVAWASKTGVVNGYSAEAFGPDDAITRQQLAVMLCRFANLIGMDT
KAHVSALDAFTDADQADTWATDSLAWCVKTGVMKGRGDDTLDPKTNITRTEATVMFDRLI
GLMK

Enzyme Prediction     

No EC number prediction in MGYG000004725_01413.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE8	1009	1333	2.2e-34	0.78125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0737	UshA	2.40e-76	1593	2111	5	504	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	4.18e-72	1562	2108	611	1133	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09558	ushA	2.19e-67	1594	2122	14	548	bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07408	MPP_SA0022_N	9.88e-51	1615	1861	1	242	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	3.96e-50	1615	1859	1	237	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
ADL35206.1	1.20e-108	964	1421	689	1133
APU68882.1	9.81e-108	75	1403	291	1486
AFK85374.1	2.87e-98	1014	1411	1331	1724
ACU08321.1	5.32e-96	872	1416	484	995
AVR45655.1	8.60e-94	75	1394	26	1370

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1A_A	1.21e-41	1615	2125	30	531	Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
4H2B_A	1.31e-31	1610	2092	22	519	Humanecto-5'-nucleotidase (CD73): crystal form II (open) in complex with Baicalin [Homo sapiens]
5H7W_A	1.88e-31	1615	2082	5	487	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	6.11e-31	1615	2082	5	487	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
4H1Y_P	1.31e-30	1615	2092	26	518	Humanecto-5'-nucleotidase (CD73): crystal form II (open) in complex with PSB11552 [Homo sapiens],6TVE_P Unliganded human CD73 (5'-nucleotidase) in the open state [Homo sapiens],6TVG_A Human CD73 (ecto 5'-nucleotidase) in complex with AMPCP in the open state [Homo sapiens],7BBJ_A Chain A, 5'-nucleotidase [Homo sapiens],7BBJ_B Chain B, 5'-nucleotidase [Homo sapiens],7P9N_A Chain A, 5'-nucleotidase [Homo sapiens],7P9R_A Chain A, 5'-nucleotidase [Homo sapiens],7P9T_A Chain A, 5'-nucleotidase [Homo sapiens],7PA4_A Chain A, 5'-nucleotidase [Homo sapiens],7PB5_A Chain A, 5'-nucleotidase [Homo sapiens],7PBA_A Chain A, 5'-nucleotidase [Homo sapiens],7PBB_A Chain A, 5'-nucleotidase [Homo sapiens],7PBY_A Chain A, 5'-nucleotidase [Homo sapiens],7PCP_A Chain A, 5'-nucleotidase [Homo sapiens],7PD9_A Chain A, 5'-nucleotidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	8.99e-45	1605	2103	659	1159	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
A9BJC1	2.20e-44	1615	2119	24	494	Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
F8S0Z7	8.23e-33	1615	2082	44	526	Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2
Q05927	1.68e-32	1615	2092	29	521	5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E PE=1 SV=2
B6EWW8	8.30e-32	1615	2082	44	526	Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 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
0.001126	0.995907	0.002353	0.000222	0.000179	0.000169

TMHMM  Annotations     

start	end
7	29