CAZyme Information: MGYG000000129_01005

Basic Information

• Species: Marseille-P4683 sp900232885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Marseille-P4683; Marseille-P4683 sp900232885
• CAZyme ID: MGYG000000129_01005
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1787		197316.02	4.0891

Genome Property

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

• Gene Location: Start: 41500; End: 46863 Strand: -

Full Sequence      

MKKSRKILALALSLSMLCTAALPLTAGAEQSISASDTLNHGVYVEYYEVEPNAPYDLVTS
DLKNTGFVQTINFGDMNSVGLEMVGRNIYYGARLHFYIIPEESGNYVFNPDADDYVRLWV
NGNQIIQGGWGGNYYAERPSKSVYLEAGEKYEIQLDYAQITGGAGLTLYWSKDGAKKTVV
PADVLYLPEGMGPVDFPEIPEVGTGKIYAVATSHLDTIWNWTYETTIGEYIPKTMRENFD
RIENSPNYKISFEGARRYALMEEYYPEEFEQVKEYVAEGRWNTAGSSWENGDQNGPSPEA
LIRNALYGNQYFADTFGNDKRSKDIYLPDCFGFGYAMPSWMTHMNLISFMTQKLTWGNAF
PNEQLPFDIGRWIGPDGNSVMASINNGSYTSSVSSSRREDSWTLNKLNQNKAWGYYGTTF
FYGVGDTGGAIGQDSINIIDNDIALNGTEESDGIDVISSTTDQWAREMTEEQKAAAPTYD
GEMLLKEHGVGSWTSRALGHRWNSRNELLGVAAEKSAVAASWLGTEEYPMDAFNTAWTRV
IGHQFHDDITGTSYATEYVRSWNDYMLSLNQFGNEYENAVGGVASAMDTSVAEGTALVVN
NPVAIDRNDVVEATVTMDSDCEYVRVYDDDGNEVPSQILSKDGNVFEIAFTAEVASMGYR
VFDVRPADSASDIDTGMSVTANSLSNDKYDVTIDENGDISSIYDKTLDKELLAEPIRLGQ
LNDTETEWPAWELKFSDYADKDAREYVADKASDIEIVENGPARVALKITREYGNSSYEQI
VSLDNGGEAVEVQNVIDWHEKSTMLKATFQLNAANETATYDLGLGAIERTNNTQWQAESP
AQKWADLTDESGEFGVSILSDSKNGWDKPYDDTLRLTLIHTPTGDYLSESHQSNLEQGEN
RFGYAIYGHANTYGEAETQQQAQLFTEPMVAFQTVKHDGSLGSNYSFASISNDDIIVRAV
KNGEVGEGLENQGDEIIVRFNEGANKAASDVEFSIGNGIASVREVYGSEETMPEDVSAEQ
GAYELKDGKLVFDMKPYGIRSFAIKLKDSGIDVAADESASIALPYNKDIYSSNSNKTDSN
MNAKREAFPSELVPSVITAAGVDFVMGDKTDGADNAIVANGQTIEIPEGYNKLHLLAFST
NGDHNATFKVGDSVQTISIADYSENIAEWEVYPVNTDAYIKQDDVAYVATHRHSNGGDQI
AANTYMFQYELDIPEGATSVVLPEDNTIFITAATAVNEQAPGEIVTEMYDSREYVETQEA
TGQFEGYSGFEEDDPVPYESQTGNCVKIDNAKCEVVADENAHSGSNVVRLTGTDTVSQSG
QGISHVYFDLYPASGFTIQPDTYIEYWIKPNNEISRHAGLDIGTDDYDASYNATMRDNAK
CVDQNGTQMHPKNARGEVGEWTRIRCDIGKYFKPGTKVTSLWFVYDNPEGQGEIDVCIDD
IFIGIDKTREDLQSLVDEVNSLNREDYYENGFVNVDEVMERAESALDDETTTNQMFSIIY
DKLQKAVDQLVPKVADKSPLIALMEEVNAIDRTLYTEESLAILDKAIAKGQKVLDNAYAS
PDDVTIAIEDLNNAVAALEKQPEFYATTDKDRYEVNETITATIITSKDARGLSLRNERDK
AIGLTSISSRISGDKKIWTVTFSVGSNGTRALNVLANTLTDGWVETGITVNFQVGDPKPV
EPEDPTPLQVLSLDFDKSVVGVNETVQATVTTTTSVDGIVLRNERDKGITISNVEYTDNK
DVRTWTFDFSVGSAGFRDLTVKGYSGTRTNIESWTENAVSQALIVTK

Enzyme Prediction     

No EC number prediction in MGYG000000129_01005.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	206	478	6.8e-49	0.9628252788104089

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	1.10e-64	206	436	1	222	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	1.51e-59	206	1046	199	941	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam07748	Glyco_hydro_38C	3.33e-38	684	883	1	199	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	1.03e-35	207	429	2	215	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	1.92e-33	206	429	1	221	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
BCI61375.1	0.0	1	1787	1	1787
BCI61374.1	0.0	1	1785	1	1789
BCI60126.1	0.0	197	1673	32	1485
BCI61027.1	0.0	200	1512	42	1323
BCI60986.1	0.0	279	1513	4	1208

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	6.70e-42	206	1046	282	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	1.08e-41	206	1046	282	1077	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]
6QE7_A	6.69e-11	82	229	39	188	ChainA, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus],6QE7_B Chain B, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus],6QE7_C Chain C, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus]
6QDI_A	1.77e-08	60	208	15	159	ChainA, PA14 domain-containing protein [Acetivibrio clariflavus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	1.03e-49	206	1042	256	1082	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9NTJ4	1.09e-42	115	964	145	964	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q9UT61	3.26e-41	206	1046	282	1077	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q91W89	1.26e-38	207	964	252	963	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	2.74e-35	207	1047	252	1036	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 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
0.000510	0.997081	0.001531	0.000443	0.000232	0.000181

TMHMM  Annotations     

start	end
7	29