CAZyme Information: MGYG000002403_00152

Basic Information

• Species: Robinsoniella peoriensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
• CAZyme ID: MGYG000002403_00152
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1044	MGYG000002403_6|CGC1	120569.62	5.0074

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002403	7202103	Isolate	not provided	not provided

• Gene Location: Start: 28259; End: 31393 Strand: -

Full Sequence      

MFLTDNKLEARTQQLKGYRYREVMHLGDFLVSEDRQGTVNPEVPADYDGWDSMQVNDTWQ
GRDRYLWLHKDITIPEEWKGKKVLGIFDYGNTGAGNNSGFESLLYVDKTPYQGVDVNHKE
VFFEEEHLGRSLDLTFRLWSGLEGGGAPVPQEHRINQADLAWLDEKTDDLYYLSSMIIDA
VKNLHDDDPVKHQLRTALDSALECIDWSYPGSSSFYESVHLADEKINEKIESMGKDARIL
VKCVGHTHIDVAWLWRLKHTREKCSRSFSTVLRLMEQYPEYVFLQTQPQLYEYIKNDFPQ
IFEKIKEKVKSGQWEVDGGMWVEADCNITSGESLTRQILIGSKFIKDEFDKEVEYLWLPD
VFGYSWALPQILKKSGIDMFMTTKISWNQYNRMPHDTFKWKGIDGSEILTHFITTPDPWS
TPGSWFYTYNGQLTAKTVKGVWDAYSEKDMNKELLISYGYGDGGGGVNRDMLEQRRRIDK
IPGLPALKTSTAGAYFKDLKDTVKNTDQYVHTWDGELYLEYHRGTYTSQGYNKRMNRKME
YLYGNTEWLTAMAALSQGDLKNANQEALTEGWKILLTNQFHDIIPGSSIHEVYEDSKVDY
EKARDIAREVEKEAYGIILDESEDTYTVLNHASWKLDGIIEIPETGILRCMDQSGNNLKM
QTGTEGTYVQTGEIPAMGFAQIRCVKESGGADNSGLENDSSYIEGKSIETKYYIIDFNDH
GQISRLYDKDAKREVLAEGTKGNVLQMFEDKPLGNDAWDIDIFYQQKMKEITDLQKFQIV
VSGPLMTVVHLEWKYMNSTVEQDIILYEDNRRIDFRTKVDYHENHQLLKAAFPVDIRTTY
ATYDVQYGNVKRPNHWNTSWDQARFETVAHRFADLSEHDYGVALLNDCKYGYDVKDNILR
ITLLKAATHPDHLQDQGLHEFTYALLPHMGDCINGRVIQEAHRLNRPLELRKGTAKLPYE
SFLVFDCDHVEADAIKKSEDGNYLVVRFHEFAGSRCQAAIKPGFQFTAWAEGDLRERPIQ
EFCSETEISIMLKPFEIKTILFKC

Enzyme Prediction     

EC	3.2.1.24

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	241	509	4.2e-85	0.9442379182156134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	0.0	18	1042	14	941	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	5.81e-124	243	500	4	250	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.
pfam01074	Glyco_hydro_38	1.04e-92	241	513	2	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
pfam07748	Glyco_hydro_38C	6.07e-79	708	912	1	203	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10813	GH38N_AMII_Man2C1	4.88e-75	241	500	2	250	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWY97338.1	0.0	1	1043	4	1039
QBE96344.1	0.0	1	1041	1	1037
ANU77101.1	0.0	1	1041	1	1037
QQQ94677.1	0.0	1	1041	1	1037
ASU29899.1	0.0	1	1041	1	1037

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	3.51e-132	66	1039	104	1072	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	4.77e-129	66	1039	104	1072	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	8.98e-124	2	1037	54	1089	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
2WYH_A	3.37e-13	241	906	28	779	Structureof the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYH_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYI_A Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS],2WYI_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS]
1HWW_A	2.46e-08	238	602	50	458	GOLGIALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE [Drosophila melanogaster],1HXK_A Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin [Drosophila melanogaster]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	5.81e-163	67	1042	83	1084	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9NTJ4	2.07e-148	54	1041	68	1032	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89	5.11e-142	54	1041	67	1031	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	6.22e-137	54	1041	67	1032	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9UT61	5.92e-132	66	1039	104	1072	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000062	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002403_00152.