CAZyme Information: MGYG000000057_00291

Basic Information

• Species: Bacteroides sp002491635
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp002491635
• CAZyme ID: MGYG000000057_00291
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1318	MGYG000000057_2|CGC2	147526.45	7.2987

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000057	4370351	Isolate	United Kingdom	Europe

• Gene Location: Start: 59353; End: 63309 Strand: +

Full Sequence      

MPWTVFYISMSRICTVREWSPGYLCAEAGHRILVLCLKVADVCPKVADVRFKLWDFYPKA
WDRTESMFSQTFVYVLPNFATSIPELFHLCPVCQGIIFYSMKTNNSRTMKRRPMLAGKAR
LIAGAVMLAVAGGHLSAQTAAPQKAKAYMVADAHLDTQWNWDIQTTIKEYVWNTLNQNLF
LLNQYPDYIFNFEGGVKYAWMKEYYPREYELMKAFVKAGRWHVSGASWDATDTLVPSIES
FIRNIMLGQEFYRKELGVESTDIFLPDCFGFGWTLPTVAAHCGLIGFSSQKLDWRNNPFY
GKSKHPFTVGLWKGVDGASVMLAHGYDYGRRWDNEDLSENKYLMELSRCTPLNTVYRYYG
TGDVGGSPTIASVASVEKGIKGDGPLKIISATSDQLFKDYQPYDAHSELPVFDGELLMDV
HGTGCYTSQAAMKLYNRQNELLGDAAERASVAAALLGTAEYPGKSLTESWQRFIFHQFHD
DLTGTSIPRAYEFSWNDELLSLKQFSGILTHAVGSVAGKLDTRVKGIPVVLYNASGFKAA
DVVTMEVKAPRFPKGVAVYNEQGKQVASQLVSYTDGKVRLLVEATVPANGYAVYDVRLSG
EGRKVSAVEATSIENSLYKLTLNENGDITSLLDKKNNKELVKAGKAIRLALFTENESFEW
PAWEILKKTVDATPISITEDVKMTLCENGALRKTLCVEKRHGDSFFRQYIHLYEGILAHR
IDFTNEVDWQSANALLKAEFPLNLNNEKATYDLGVGSVQRGNNSLTAYEVYAQYWADLTD
ANGSYGVSIMNDSKYGWDKPDNNTLRLTLLHTPKTKSNYAYQDRQDFGRHTFTYSLVGHT
GALDVVRTRENAELLNQRIKAFAVGKHRGELGKSYSLAFSDNRNVLIKALKKAESSDEYV
VRVYEAGGKQAQKASIVFADNLVAAVEADGTEKTIGKAAFSGNRLEVSVNPNGIKTYKVR
FASNKKVQTVARPLPLAYDKKCFSWNEFKAAADFEAGYSYAAELIPTEMNVNGVPFKLET
REELNGMACKGNVLKLPADCAYNRLYILAAAASDKDVKGIFRTGKSVQEIIVPSYTGFIG
QWGHTGHTEGYLKDAEVAYVGTHRHSGEGDQPYEFTYMFKFAIDLPEKATEVVLPDNKDI
VIFAATLTNVAAASVCPVSELFRTANKCNRYQTESSTERVNILKQDMVMGYSSYVNEKEK
PAFMVDGDENTKWCAIAEMPHYVDFDLGSERSINGWKLLNAAGENHSYITSSCFLQGKTD
KNSEWRTLDYVSGNGKNVLNRTLNKPESVRYLRLLVTQPMQSASGKDVRIYEMEVYAK

Enzyme Prediction     

EC	3.2.1.113	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	146	399	5.4e-51	0.9219330855018587
CBM32	1193	1313	5.7e-17	0.9032258064516129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	1.86e-83	146	403	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	1.76e-77	148	961	201	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam07748	Glyco_hydro_38C	4.34e-42	613	814	1	199	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
pfam01074	Glyco_hydro_38	1.83e-41	146	399	1	254	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10813	GH38N_AMII_Man2C1	7.63e-39	148	399	3	248	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
QBJ18498.1	0.0	109	1316	1	1208
QMI79903.1	0.0	109	1316	1	1208
QPH58799.1	0.0	109	1316	1	1208
QUT61522.1	0.0	109	1316	1	1208
QQA30012.1	0.0	109	1316	1	1208

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	8.58e-71	144	970	280	1086	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	2.36e-69	144	965	280	1081	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	8.14e-52	148	961	305	1096	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
5KBP_A	3.01e-14	144	902	6	846	Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
3LVT_A	1.17e-13	141	902	3	846	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	2.52e-83	146	964	256	1087	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9UT61	4.06e-69	144	959	280	1075	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q91W89	1.66e-60	148	908	253	980	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q9NTJ4	2.23e-60	154	908	260	981	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
P21139	9.01e-59	154	908	259	981	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 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
1.000025	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000057_00291.