CAZyme Information: MGYG000000129_01036

Basic Information

• Species: Marseille-P4683 sp900232885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Marseille-P4683; Marseille-P4683 sp900232885
• CAZyme ID: MGYG000000129_01036
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2271		248783.6	4.1561

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000129	2720267	Isolate	Canada	North America

• Gene Location: Start: 81438; End: 88253 Strand: +

Full Sequence      

MRKATQKALSMALCLSFLATSAIPAVTASAEDGNSKPKMYAVANSHLDTAWNWPLETSIQ
SYIPNTIKQNIELLKKYPEFNMNWEGVYRYELVKQYYPDLYEELKTWIDAGRWFPTGSVY
ENGDVNVPSPEALMRNILYGNKFLEEEFGMVNTDIYLPDCFGYGYALPSIASHMGLLSFS
GNKLKWSNDNYLPFDLGNWVGPDGSTIVASLNCESYLSGFDSDINIGSKGQSWLENIMSP
YTGLSGSDIARRIKYYGTGDVGGGVGEDKVKNLVEAMARNNTDGLFEVVSAYGGQMVEEM
TEAEKAALETYNGELQMRWHGNGTWTGQALQKYLNRKSELLADKTERSASAAAWLGVNNY
PAEKLKAAWKRVVALQHHDVLPGTSIAEVYEQATNDYIIALNQFAEEYETAAGGIASTMD
TRVAEGVPVVVNNPVSEDRNEPVEAEVTMEEATQYVRVYDASGKEVPSQVLSTDGNKVKV
LFLGAAPSNGYSVYNVKASDSPCDMETGLSITNNTLENNRYKVEINENGDISSIYDKEND
KEILEAPITLQQFGNHVSNYGAWEISLDDWEKGVTSEVGGENLKVTIEENGPVRVALKVE
RTHRASSFAQTIELSIGDTEDRVDVDNEVMYGERSSYMKAAFPVTVSNENATWDLGLGTI
ERDTDDEYQYEMVGQQWADLTDEDGSYGVTILNDSKYGWDKPDDNTLRLTLFHVPEKERN
SSKADRRDFGDNRFTYSIMGHTGDWREGKSQYMAQNLNQPMTAVQTTSHAGTMGSEFSFA
SLNTDQAMIKAIKKAEDTDEIIVRVYELYGQDAEGVTLSMGDGIESFRETNGYETSVSDS
TAKLVDGKLVFDMGAYTPKTFAVKLKDKDTSAVTPTYQSIDLNSQFNKDIISFDSNRSDG
GFGENGYTFPGELMPESITTGGVTFQLGSSEDGKNNAIEAAGQTIALPEGTTKVHLLAGS
QGDDADFTIKVGDQDQVISVQNMWNYVGEWDQYCLNRYGGIKRDAIGLLVDHTHKPSEDR
YNDHGYLFDYTIDIPEGVTSITLPEDSNLIVAAATAQTNETYDSFITSPLYPEKEEAAVH
TLSVEGVDADLVTGIGEYRTGNPVSINYKGEAADVTWIGSNGTTYEGASIQINMPDEDLT
LTPVITPFESEDLAKGKTVKASGETKASEAASMAVDGDDTTKWCDTTSGNKWLEVDLGEP
MVIDTYVLKNAGFGGETEAWNTADWQIQVKDQDGNWVTVDQVSENPLDSYTGKIRPVYTQ
YIRLYITAPTRQPTGNSAARIYGFELYQQGDYEGQVVVSNPTLQMGKGGQNVKVTLPAYS
DKEGNKVTISAVVKDEKGQIKLDKKQDVALGSNGWDTYTQYVDLYDAVGGIAKTDTLELV
ILNAEGEEISDVITVENLGDITFADPFQRLEAEDYSTWSGGNLKVENSTTSEGETIRNIG
GTYPNAWIAYQNMDFGTGANMLSIRYANNSGRCKSDAKIEVRLGSEDGKLVGTIDIPATG
SDWSIYGTATGKLDETITGVQDVYLVMRGTTPDSNPYIANFDYFQFNYERDAFSTIENED
YDEWSGGGLKTEAGDNGTVLAGTYNNAWVKFDNVNFGDGAKAASIRYCAAESRCAADSRV
EIRLDSVDGPLAGTIQTPPTASGWGTFTTVEGGLDQTVSGVHDVYFVMKGATDSSHPYIG
NFNNFVFIEGQAVEKQVQRVEFEDYADWKDSAMKTEAGGTGTVVANTYPNDWLHYTVDVG
NNSMTEITVNYSNNSGRCKTDAKVEVRLGAPDGELIGTVQTPPTASSWGTFGTASTVLSK
PITGKQDIYLVLVGTTPDSNPYIGNFDYFELKGEEIPETPASVGVEFEDYADWKDSAMKT
EAGGTGTVVANTYPGDWLHYTMDLGNNSMDEVAINYSNNSNRCKTDAYVEVRLGSPDGEL
VGTVQTPPTASSWGTFGTATASLNKTLTGKQEIYLVLKGTTPDGNPYIGNFDYFELRGVK
NPDVSIDSVGDVEGKTVPYGTAFEDLDLPETVNVALSDGSNREVEVQWQQGDYDANTAGT
YTLNGTLVLTEGILNPQELSASIQVTVEEKVQTDEFSIDFEKDYYQVNEEMTVTVVTPKD
VNNIQVVNERGNAISTLKLSSIFDGQKKIWTMTIKVGSTGNRTFGLKAYQNGAWVMTNVT
DQVTVGNMPIDTEVKPFIYKADFSATEAKVNETFTATVVTSTSIDKLAIVNERGKYVSFK
QVGYEDQGDKRTWTVELSVGSAGFRILSFKAADVNGNWLPQTAECSIKITK

Enzyme Prediction     

No EC number prediction in MGYG000000129_01036.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	38	222	4.2e-48	0.6914498141263941
CBM6	1410	1547	2.1e-25	0.8695652173913043
CBM6	1557	1687	8.5e-23	0.855072463768116
CBM6	1702	1832	8e-21	0.855072463768116
CBM6	1848	1976	5.5e-20	0.8405797101449275

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	1.28e-68	20	834	169	918	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	1.24e-65	38	219	1	181	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.
cd10813	GH38N_AMII_Man2C1	2.08e-38	39	209	2	171	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.
cd10812	GH38N_AMII_ScAms1_like	1.12e-37	40	208	3	170	N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. 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 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1.
pfam01074	Glyco_hydro_38	2.22e-36	38	207	1	170	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI61304.1	0.0	1	2271	1	2272
BCI61027.1	0.0	2	2256	5	2115
BCI60986.1	3.14e-308	108	2271	1	2005
BCI60126.1	8.75e-293	3	2253	2	2088
BCI61375.1	2.32e-282	38	1107	206	1289

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	3.93e-64	31	865	275	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	6.33e-64	31	872	275	1084	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	6.06e-46	31	813	294	1039	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
5M77_A	1.94e-15	1405	1597	388	573	ChainA, Alpha-1,6-mannanase [Niallia circulans],5M77_B Chain B, Alpha-1,6-mannanase [Niallia circulans]
2WYH_A	6.88e-13	38	820	27	887	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	7.64e-73	29	810	247	1031	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9UT61	1.42e-63	31	865	275	1077	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
P21139	1.14e-57	33	810	246	981	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9NTJ4	5.94e-56	33	810	247	981	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89	1.04e-55	33	810	246	980	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 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
0.000252	0.999023	0.000159	0.000215	0.000167	0.000144

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000129_01036.