CAZyme Information: MGYG000000026_00156

Basic Information

• Species: Catenibacterium mitsuokai
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium mitsuokai
• CAZyme ID: MGYG000000026_00156
• CAZy Family: GH92
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
778	MGYG000000026_3|CGC1	85347.25	6.2124

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000026	2527406	Isolate	United Kingdom	Europe

• Gene Location: Start: 12176; End: 14512 Strand: -

Full Sequence      

MKKQNTLIALSVLSAMSLTAVSPIALNSFSNVVAVSANQSSAQGTVVMNQDADMKYLDTN
VDPADGTLAKDKWGQYTGWTRVYKNGDNASLNGQYNDTAWKTAKGEFSTQTGTLNKDSRA
YFFRGYFNVDNTSAVRGIHLNFGYKDAVIVYINGQQLTAFNVPDEGYRTNASGNGSHKDN
MGYGSKQTFTEAQTADLYFRDIKDMLQNGQNVISFEIHKTNANSEGYFKMNELGINPDES
LLPARSSLKAISLSVGSTPSELNINWFSTDSSNGQVQYAKKADMHGAFPEDKAVTVVAKM
SKAQADGYYANKATMNNLEENTSYIYRVGNNGQWSDTYTTTTKASGNFSFLFAGDPQLGS
SGDLASDKDGWKNTLNLIKKSSLFKNVNFIQNAGDHVEAGKNESQYDAYLSNYEGSVVYS
TPFANAVGNHDNSGTAYNDHFNLPNVSQLGNSGEGNAQGDYYYIYNNTLMMVLNSNNRST
AQHEEFIKNTIAKTKDNKDIKWKIVVFHHSIYSSASHASDNDILARRDTLAPMLSENGID
LVLMGHDHVYTRSMLMDGSKALKEESFDQNGQPIHEVTNPKGLTYITANSASGSKYYEFT
NNLTGDYIAVKNQEHTPNITKLDVSDNQLKIVTYRTTDLSVVDDFTINKTTTDTVDKTEL
KNAVDDASKIDSKDYTADSFSKLQDALVKAKTVLNNKNASQDEVNDAFNALKSAKDQLEK
KSVVVTPNKDHSSNDKTQTKNNAVKTGDTTQLTALSVAATVAVVTGATIMIKTKKKEI

Enzyme Prediction     

No EC number prediction in MGYG000000026_00156.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00839	MPP_PAPs	7.88e-15	362	647	11	294	purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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.
pfam16656	Pur_ac_phosph_N	1.31e-13	251	342	4	94	Purple acid Phosphatase, N-terminal domain. This domain is found at the N-terminus of Purple acid phosphatase proteins.
pfam00149	Metallophos	5.43e-12	348	550	1	191	Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.
PLN02533	PLN02533	7.67e-11	211	552	18	336	probable purple acid phosphatase
cd07378	MPP_ACP5	2.52e-10	385	548	35	217	Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. 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 MPP superfamily 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). 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
BCI59828.1	2.50e-124	40	651	776	1366
QNL45026.1	2.76e-110	47	649	1570	2148
BCL56920.1	6.42e-07	655	722	1277	1344
AQM59543.1	8.94e-07	623	728	1889	1978
AIY85170.1	8.94e-07	623	728	1889	1978

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WL80	5.95e-07	261	559	79	398	Uncharacterized protein MT2654 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2654 PE=3 SV=1
P9WL81	5.95e-07	261	559	79	398	Uncharacterized protein Rv2577 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2577 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
0.097196	0.883171	0.018134	0.000772	0.000350	0.000352

TMHMM  Annotations     

start	end
7	26