CAZyme Information: MGYG000004703_00382

Basic Information

• Species: Prevotella sp900556275
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556275
• CAZyme ID: MGYG000004703_00382
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1835	MGYG000004703_7|CGC1	204446.65	5.5046

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004703	2398084	MAG	China	Asia

• Gene Location: Start: 10766; End: 16273 Strand: -

Full Sequence      

MRKYFLEFLSLLPMIALADGNNNYKQLSLTGYNADLVLTTGEDFRDPLDSQGWCFFSEYK
GLRGGLPERIRGMFSDVPYVFNDFKSNCAFLLSENKNKSNVVYGRQQTITLATPTKAKSL
WLLATAADGTARINVTVKYTDGTTDNAVSLEVNDWKSNQNTNTAFWQLGRINSSGRKEND
YTFALYEKVVPVTNSNKNIASISVELPETGKEVAIFAVTASTNEAPGSLKDKKLFFLSNS
HLDTQWNWTVKTTIGEYIKNTLTNNFDHFDNSETSNFNFNFEGAIHYMWAKEYYPEYYAR
LKNYIKQGRWNIAGGSIDANDVNIGSAESQIRNFLYGQNFFMNEFGQRGGRDIMLPDCFG
FPWSLPTVAAHCGMKYFHTNKLSWNSAYAYNKLPRYARWIGTDGSELLAVLKTNPYDDHE
KFRKDMSSDSEMTNEINSNNTTYGIPAALKYVGPRSDRGGGLDKETAVWLSKSVDGTGPQ
SVAINSSTEMLDQIFHMGYDKLPTINHGLPMRAHGVGGYTSRCMLKFWMRKGELLGSAAE
GASVAADWLKTLPYQQSTLSNAWIRLLWHQFHDDIPGTCINEAYRYSVNDQLLNQLDFSR
TLNNAVGAVASNMKTDWCKNIPVVVYNPISQNRTDIVEATVTMPAGTEYIEVKNPNGQTV
ASQVLERNGNDIRFIFLATVPSMGYATYNVAPSATAFSSNNGLSVSESSMENSRYRIKIN
QNGDVSSIIDKKQSNKEMLSAPIRLAMLFDESLTWPSWEIHGDQLQKAPREYVDKEGLSV
EVVENGPLRASLKVVRQKNGSEFYQYIRMYSAGSADRIDFVNEVNWQTKERMLKAVFPLS
ASNAEATYDLSIGADVNKNSTSYSTDTNNTDAICEFLGHRWADVTNSDGAFGVSILNDCK
YGWDKQKNNEIRLTLIHTPKVGGSYSYQGDQDLGLNKFTYSFFAHSGKWNADTQWEADKL
NQPMYAYQTTKHTGNMGTDFGFVKVNNNNVAVKALKKAERSEKTIVRFYELTNNAQSVEV
EFPANIISAEEVNGVEELVGPATFSGKKLQFDIERFHPKTFALTFAEPTGPATIVDTPVS
FSVELDYNIDVISPNTNRKDAEISKAYPAELVDDNITADGIVFKMGSKTAKAKNAVKCVG
QTITLPTVTNGKKLYLLAASLNSDGSEATFDVDGKATSLRIEYNGGMVGVWSNSADVQKH
YRTENTAFTATHNHDVAGNKDGIFDYLYMYKYVIPVLANSKTLTLPDNPDILIFAITVSD
NTNDDTKAISNTVNVLNHTDTEDPFQEVYHEDPALKPSSCTASSYTNSSESPEKAADGDE
STKWCDNSSAVKWLEYKFDKQVTVSGWRVMNAGSEGEQHIASEYKLQRFVNNGWVDVDGV
FDNTTNTTDKVLEQPFVTTAVRLRIITPGHNDPKDAARIYEFKVFGHEATDEDMTMSQII
SRRPDYGYGKTVARVVASTGRTKASEDPYYILDSDRTTKWCYNGSVSMPYVDVKLADVYS
LDRFDIYDSKTMENYANSDEFTILVSMDGKTFNEVASKSGVASENIHTCKLAKPVDARYV
RLQISKGGGGAVRVYGFDIWGTFKEKSADEPGKPVSLDKTILGAFNVKHLDESPLNLVDG
KYDNIEYTWNFDNMGNNGKINWVVVDLESQYNINKFIIRDANTSNVNNFTGYRIYVSNTA
PTEKEMNNFKSIAGGSKWTRVVPLTTDNNATKTITLDTPSKAQYVKLEIPVANVKDSAMV
REFEIYGELVPTGISVVGNSGDINVYPNVVDRGQDIHVTAPQNAKYVLSNVGGCVVSQGV
VNNEQTVATNEMAPGIYIIRVKSGVQILNKKIIVR

Enzyme Prediction     

No EC number prediction in MGYG000004703_00382.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	234	434	1.2e-45	0.7323420074349443

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	9.98e-70	230	1037	196	919	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	2.30e-65	233	465	1	220	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	3.12e-37	233	461	1	221	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	7.31e-37	234	461	2	216	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.
pfam07748	Glyco_hydro_38C	4.59e-34	710	920	1	199	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
QUT74823.1	0.0	227	1428	21	1209
BBL08592.1	8.65e-257	233	1425	24	1196
BBL11384.1	8.65e-257	233	1425	24	1196
BBL00551.1	3.35e-256	211	1425	2	1196
QUU05389.1	5.71e-241	214	1425	10	1204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	1.01e-57	234	1037	283	1045	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	2.99e-57	234	1037	283	1045	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	7.23e-43	234	1036	304	1059	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
Q9UT61	4.12e-57	234	1037	283	1045	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q54K67	5.45e-56	233	1061	256	1082	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q91W89	2.13e-46	237	1010	255	977	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	1.49e-45	241	1010	259	978	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9NTJ4	1.49e-45	241	1010	260	978	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 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
0.000329	0.998867	0.000228	0.000198	0.000189	0.000162

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004703_00382.