CAZyme Information: MGYG000001306_02006

Basic Information

• Species: Phocaeicola coprocola
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprocola
• CAZyme ID: MGYG000001306_02006
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1202		135068.67	5.6715

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001306	4295617	Isolate	not provided	not provided

• Gene Location: Start: 18336; End: 21944 Strand: +

Full Sequence      

MKQPVVLFASLCFLASEAMQAQNAQNSPKAYVVSDAHLDTQWNWDIQTTIQEYVWNTLNQ
NLFLLRKYPDYVFNFEGAVKYSWMKEYFPTRYEELKQRVKEGRWHVTGSSWDANDVLVPS
AESVLRNILYGQNYYRTEFGTESTDIFLPDCFGFGWTLPSLAHHCGLIGFSSQKLGWRNH
PFYGDKKYPFTIGLWKGIDGNQIMFAHGYDYGHRFKDEDLSDSEELKQLVKESPLSTVYR
YYGTGDMGGAPTIISVRAVEKGVKGSGDIEVVSATSDQLYKDYAGKHEQLPVFDGELLMD
VHGTGCYTSQAAMKWYNRQNELLGDAAERAAVAAEWLNQGNYPKSELETSWKRFLFHQFH
DDLTGTSIPRAYEFSWNDELISLKQFSDVLTSSVNGVSRLLDTNVKGTPVVLYNALGFAV
NDLAEIEVEFAKAPKGIAVYNAEGKKVASQYLGYQDGKAHILVEASVPATGYAVYDVRTS
GAGVQTVKQQHADTLENSCYKLSFDANGDIVSLLDKRNGKELVASGKAIRLALFTENESF
EWPAWEVLKKTLDREPVSITHGVKLTLVEDGDLRKSICIEKKHGESVFRQYVRLYEGTRA
PRIDFYNEIDWCSTNALLKAEFPLAVSNPNATYDLSLGSVQRGNNTVTAYEVYGHYWADL
TDRKGDYGVSIMNNGKYGWDKPSDNTLRLTLLHTPKTDKGYTYQDRQDFGYHTFTYSLLP
HQGELDKAEVVSKAEVLNQTLKAFQTDKHKGEMGRTFSMVSSDNPNVIIKALKKAVDADE
YVVRVYDVAGKGTQSARLTFAGKLVEAVETDGTEKEIAKAGFSDNTLEVTVKPFSLKTYK
IRLAESGMEVHQPKCLALNLPYDKKCATYNEFRSEADFESGYSYAAELLPDSITVDQVTF
RLGEQEAYNGLSCKNDTIEIPEGYNRLYFLAAAASVEDQRLQIACGKQTSEFVVPSYTGF
VGQWGHEGHTTGYLKPAQIAYVGTHRHASDGDCPYEFTYMFKFGMDIPKGVRSVVLPQNE
NVVIFAATAVAEDRSPVKPSTKLFRTNNHEELSELVSGNKMISGENLLKNAKLTRWSAYV
NEKERPQAAVDGDLSTKWCDIAGLPSFLEFDLGKAEKLTGWKVVNAGKENGSFITSQCFL
MGRNSVDEDWQTVDFFDGNRSNVVLRTITSDKAYRYLRMVVTRGTQAASSKDVRIYEVEV
YR

Enzyme Prediction     

EC	3.2.1.113	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	29	281	9.7e-53	0.9182156133828996

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	1.89e-83	29	286	1	252	N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl-enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
COG0383	AMS1	7.93e-81	26	843	196	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam01074	Glyco_hydro_38	7.59e-44	29	293	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10813	GH38N_AMII_Man2C1	5.34e-41	31	252	3	218	N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase.
pfam07748	Glyco_hydro_38C	4.48e-40	495	698	1	201	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUA16945.1	0.0	1	1202	1	1205
CAH06062.1	0.0	1	1202	1	1205
QCT76910.1	0.0	1	1202	1	1205
AKA50432.1	0.0	1	1202	1	1205
QUU05389.1	0.0	1	1202	1	1205

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	3.48e-71	16	843	270	1077	Structureof S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_B Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_C Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_D Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-]
7DD9_A	1.23e-70	16	853	270	1091	ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]
5JM0_A	1.08e-56	13	841	286	1094	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	1.70e-87	17	840	244	1083	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q91W89	2.92e-79	14	838	236	1029	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	8.27e-78	14	838	236	1030	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9NTJ4	1.51e-77	14	836	237	1028	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q9UT61	1.21e-70	16	843	270	1077	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 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
0.000226	0.999130	0.000170	0.000173	0.000146	0.000137

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001306_02006.