CAZyme Information: MGYG000000932_00420

Basic Information

• Species: UMGS577 sp900543525
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS577; UMGS577 sp900543525
• CAZyme ID: MGYG000000932_00420
• CAZy Family: GH92
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1077		117217.05	5.0312

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000932	1983140	MAG	Germany	Europe

• Gene Location: Start: 930; End: 4163 Strand: -

Full Sequence      

MGDTENYNKWLKRSENWMNIWNPDVTDNGYSGFIWPKAADGSWISDSGMRGPGYWQGSWS
KYFYESTSWAYSFFMPHAIPQLIEKMGGEETFCSRLMIGLERGWINFDNEPAFLAPYLFA
YTGKPYLTTDSVTLLRSRFNLKGVPGNDDSGAMSSWYIFSSIGFFPNAGQNLYYFTSPRY
PETTIRMDSGKTLRLIANNLSDENRYIQSITINGKPYKSTMFTHDVITAGGEIVFEMGST
PVDYAKETTANITVAEVGLDAVYLDGTKCDERLHLTALDQLNRSAGAGSPALAPEGVRFT
GEYKANGTLGSRGSGFLWTNGVPTASSAGSGACVWSDSAEFSVTLEGDAQLELYVAGSAV
LEVFTADRQKLEEAAISGTGGGCRKVSLRLGCGRPETFTLRLTPAASGANARVSLAAATL
QKIECCIVSFDSMGGGAVPNQAVERGGKISPPKAPEQSGYSFSGWYADDALTIPWDFEQS
SVEASLTLYAGWKVESGVFISKMQNPDKNTVIDLSGYRDWIHFGDSSHDVIHCDRKNLSE
DMRAFGSVISVNGLREENEHNANQPFAFTWSDGTPTAAQTQPKRYFSWARDGLEMTVTVP
AGAYRADLYLSGIRSRATIEILNADRSVAAKAPQLWSNTGETRQFRVVPVQFHSAEKKTY
IIRMLVDLKKTEPENYSMAIAAATLQKSVCSLSAESGENGTVRVRGGAVQNVGETAVVTA
TPQPGYQFAGWEVVGGQLTLENPIQNPLRFSMPDGDVTLRAAFTELTAAVKGVETIATRS
TIDLVQSGNADWAYLGKSGQLIQKANVKNSAFSGAAAAVKGDLSHENMDNTNPDSPYFNW
TGGTPEKAGDQVREIVWSGEGIAFGCTLQPGQHEMDLYLSSVRTGVIAEVLNEEGQRILA
QKLWNSMGDYRPYEKVTLLFNCKKAEKFTIRLLVDQTDIHADWYSVSLYAAAVRNHTHSG
EAAGWYSGADGHWHQCLCGEVLGQTAHTSGDWILNHDGKGGHKECLICRYVTEAMSLSPG
DVDGDGAVTVSDVVALRQRIVSGVWSGWEFAAGNLDGDNLLTVSDVVSLRKRIVSGG

Enzyme Prediction     

No EC number prediction in MGYG000000932_00420.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH92	1	241	4.7e-74	0.48676171079429736

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07971	Glyco_hydro_92	2.81e-89	1	239	222	465	Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.
COG3537	COG3537	2.49e-58	2	241	501	743	Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism].
TIGR01180	aman2_put	2.36e-30	11	241	506	748	alpha-1,2-mannosidase, putative. The identification of members of this family as putative alpha-1,2-mannosidases is based on an unpublished characterization of the aman2 gene in Bacillus sp. M-90 by Maruyama,Y., Nakajima,M. and Nakajima,T. (Genbank accession BAA76709, pid g4587313). Most members of this family appear to have signal sequences. Members from the dental pathogen Porphyromonas gingivalis have been described as immunoreactive with periodontitis patient serum. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NF035929	lectin_1	3.66e-29	1	250	448	694	lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.
pfam09479	Flg_new	1.21e-12	428	490	3	64	Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI60938.1	5.39e-268	2	985	783	1842
QSW88885.1	1.41e-64	1	241	486	745
AOC96514.1	7.26e-64	1	241	296	555
ABQ06141.1	9.53e-61	1	241	486	745
AWK07539.1	1.74e-60	1	241	486	745

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F8Z_A	1.89e-29	7	246	470	719	Structureof the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],6F8Z_B Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],6F8Z_C Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],6F90_A Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron in complex with Mannoimidazole (ManI) [Bacteroides thetaiotaomicron],6F90_B Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron in complex with Mannoimidazole (ManI) [Bacteroides thetaiotaomicron],6F90_C Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron in complex with Mannoimidazole (ManI) [Bacteroides thetaiotaomicron]
2WVY_A	2.58e-22	1	241	465	720	StructureOf The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_B Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_C Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_A Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_B Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_C Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]
7FE1_A	1.31e-21	1	241	443	697	ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]
6DWO_A	1.31e-21	1	241	443	697	Crystalstructure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_B Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_C Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_D Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
7FE2_A	3.00e-21	1	241	443	697	ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D4ATR3	5.14e-33	7	238	494	741	Uncharacterized secreted glycosidase ARB_07629 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07629 PE=1 SV=1
O86365	1.44e-27	1	241	509	753	Uncharacterized glycosidase Rv0584 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv0584 PE=3 SV=1
P0DJ98	2.67e-12	422	522	79	199	Putative membrane protein Bcell_0381 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0381 PE=4 SV=1
P0DJ97	1.65e-11	428	494	665	731	Putative Gly-rich membrane protein Bcell_0380 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0380 PE=4 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
1.000061	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000932_00420.