CAZyme Information: MGYG000000129_00845

Basic Information

• Species: Marseille-P4683 sp900232885
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Marseille-P4683; Marseille-P4683 sp900232885
• CAZyme ID: MGYG000000129_00845
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2121	MGYG000000129_3|CGC4	232105.04	4.1354

Genome Property

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

• Gene Location: Start: 198600; End: 204965 Strand: +

Full Sequence      

MKKPQKILAFILSASLTAGCALPGAALAQSPGGSDATDPAPYAGEDRLYAIATSHLDTVW
SWPLEETIREYLPSTLRDNFQLFEEFPDYKFTWEGAYRYQLIEEYYPEEFETLKKYMDSG
NWNFGGSGLENGDVNVPSPEALFRNFLYGNNYIEEKFGADKRSRDVYLPDCFGFGYALPS
IAAHSNLLGFSTQKLSWGHSFENGLPFDIGNWYGPDGESIVANINLNGYVSEVGTVRGDS
GLLSKLNQNKAYGYSAASRLFGVGDMGGASGWTTVSNVLGEQALNDSEKVKVIGATTDQL
FREMTEEERSGLPSYDGEMVMREHGVGGYTSRAISKRWNRQSELMGDNAERSLVASTWLG
ATEYPQEKLTEAWTRVIAHQFHDDIPGTSTGTVYNRSWNDYMLSIKQFAAEYENGVDGVA
SEMDTSVESGVPLVVNNPVAADRNDLVEATVTMPEDCASVRVYDADGNEVASQVLVKDGN
QFDIVFMANVGSMGYRTYNVRPAATACDMESNLSVNENKLSNEKYNVTIDENGDISSIFD
KELDKELLAEPIRLALFDDTEWEWPAWELKYEDYAKKMPKDTVKDEAMDISVVEDGPARV
AIRVVRQHGSSTYDQVISLTSGGQIVAVDNVVDWDERATLLKAEFNLTSSNPTATYDLGL
GAIERGNNTDYKAEVPLQKWADLSATDDSYGVSILNDCKYGMDKYDDDTLRLTLIHTPQY
DMFHTGVRNYSGQHVQEVGENRFGFAIYGHEGNFGSGTQIEAEAFNQPMKAFQTVSHQGS
LGDDYSFGSISNENVLVRAVKKAEKSDEIVIRANEGTGEAASNVEVSLGEGIESAREIYA
SEEEIGPATVKDGKLVFDIGAYGVKSFAVTLKEPEIKTDENEMTFVELPYNIDAYSSNSD
KSDGSMNALNETYPSELVPDSVLSSGITYQMGSKEDGQNNAVAAKGQTITLPEGYNTLHL
LAASTQGDKDVTFRVGDKDVTLNIGDYKENVGCWDQYDLGIKGYVKDQDPALIATHRHTA
GVDNIAATTYMFAYDLDISGASTITLPDDDSIIIFAATAENDAAKTEAVSELYDHRERTD
EAHGFAGTSGFEPVVDEMPSESWSENNKNIDDLSCIVTDEDAASGVQSLKVSGTDSKDSD
SFVYYNVYKAAHMKVVPGTILTYQFKPLNELGRYVSMDLQFNEGSPLRDIEGAVDQDGVQ
MHPSKGRGTVGEWTTVTCDLYAAAGGKTITNVMAAYDHGPDTGEFSALIDHVFIGIPADR
ASLMSAMEEVQALDTSVYSDDDVKELARLTSLAQDLLDDPEAYEGDISYVSQNLHSLLDT
LVARDAFSNIEAEGFDSAFKSGDGVKNEGSNIGYLNDGDWVIYRNVDFGSNGAEAIELFY
SGEVRDTTGTIQVRLDSASGPLLGTISTPGTAGWSNYTLTTAALDEKVTGVHDVCLLFDC
SRNVDYFRFIEKVDKAPLTSLILQAEAVDRSNKTPASLQILDEATAEAKAIVENPNATAK
EILDSVEKMRKALASLETIKPAFERMEAEHFDDATTEGDGVKDEGNNLGYTNNGDWVMYK
NIDFADDCAVQVELFYSGEGTGEDSRVEVRADAVDGPLLATVATPPTGTWSDYRTATADL
EHIPEGVKNIYFVFRGSKNNICNIDYFLFHQGEANDVLKKTVQRAENQDLNGKTPDSIEQ
LTQALVYAKQILDDGQSTSQDRIAANNRLNQAILSLEVIRDPFDRIEAEDYDDATTQGNG
VAIQGDYIGYINDNDWVMYQNVDFRGKQAVRLEMRYAGEGTADDSRVEVRLDSVDGPLLT
TISTPPTGTWSDWETLSVDLPASDIPDGMRDVYLVFHGSKESICNVDYFLFHGNDLKADL
ESVLNEASSYDAADYTEESYDSLNQAMESAKAIQENPDASNEQYIEAITAVQEAIDSLVV
KNYVLSASADKDVYEPNETIALTIQTTADRSRIALLNENGRYVSILGMKSTYHPADNTKT
WTVKTSVASLGENRQLTIATVGASGKIVQSDTKVQFSIQAKPSGAKLISVLGAGTAKVNE
SFTIEVETTANVEQIGIYNERGNGITKQSVETCVNGDVKTFTITLSVGSTGNRIFTIKAK
DPATGRYLDDMALTLPITITK

Enzyme Prediction     

No EC number prediction in MGYG000000129_00845.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	49	310	6.3e-48	0.9405204460966543
CBM6	1724	1851	1.8e-26	0.8768115942028986
CBM6	1526	1651	8.7e-26	0.8768115942028986
CBM6	1329	1449	1.7e-25	0.8695652173913043

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	2.43e-78	25	871	174	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	1.06e-68	47	307	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.
pfam07748	Glyco_hydro_38C	5.51e-44	520	721	1	201	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	5.72e-41	47	306	1	257	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	4.90e-39	48	308	2	259	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
BCI60986.1	0.0	117	2121	1	2005
BCI61027.1	0.0	1	2121	1	2131
BCI60126.1	0.0	1	2121	1	2108
BCI61375.1	0.0	41	1326	200	1515
BCI61374.1	0.0	38	1321	186	1525

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	2.97e-67	47	871	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	5.98e-67	47	882	282	1088	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	1.56e-54	47	814	303	1016	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
1UY1_A	1.30e-19	1322	1449	16	141	Bindingsub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration calorimetry [Thermoclostridium stercorarium],1UY2_A Binding sub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration calorimetry [Thermoclostridium stercorarium],1UY3_A Binding sub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration calorimetry [Thermoclostridium stercorarium],1UY4_A Binding sub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration calorimetry [Thermoclostridium stercorarium]
1GMM_A	3.82e-18	1324	1449	1	126	ChainA, CBM6 [Acetivibrio thermocellus],1UXX_X Chain X, Xylanase U [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9UT61	1.03e-66	47	871	282	1077	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q54K67	3.31e-64	45	822	254	1035	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
P22855	8.02e-54	47	814	290	1003	Alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AMS1 PE=1 SV=2
Q91W89	1.49e-49	42	874	244	1037	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q9NTJ4	1.39e-48	42	874	245	1038	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000429	0.431619	0.567087	0.000389	0.000276	0.000184

TMHMM  Annotations     

start	end
7	29