CAZyme Information: MGYG000000032_00020

Basic Information

• Species: Hungatella effluvii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
• CAZyme ID: MGYG000000032_00020
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
826	MGYG000000032_1|CGC1	95207.9	5.0999

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000032	6969476	Isolate	United Kingdom	Europe

• Gene Location: Start: 20614; End: 23094 Strand: +

Full Sequence      

MTMIQKLTDGWKLRSCSTGQSFETKVPGTVYGTWLEQGAMKDPYWRDCEEAALAMMAGDY
EYEMSLSPDEALMGCRDIRLRFEGIDTLADIFFNGVYLGHADNMHRIWEYPVKSLMGETN
KLKVHLYSPLSFIRKAYEKTPYDGAHEAMQGFPLLRKSHCSFGWDWGPRLPDAGLFREVS
LIGVNQASICDVHIRQKHSGGIVTLTLNTTVEAAGDVACSCMLRITDPQGMSITYQMEGE
KYQFSKAVTIKNPELWWPNGYGKQPLYQAEVMVAADGELQDSWRRKIGLRTMTVNTAADE
YGNKFAHEVNGVEIFAMGADYIPEDCIRGRVSRERTKTLLEYCRDCNFNVIRVWGGGYYP
DDFFYDLCDEMGLIVWQDFMFACAVYPLTPEFEANTAAEIRDNVRRIRHHACLGLWCGNN
EMEMFLADNQWVRKPLQKTEYLIMNERIIPELLRQLDPDTFYWPSSPSSGGDFDHPNDEN
RGDAHYWEVWHGGVPFTDYRKYYFRYLSEFGFQSFPAVKTIEQFTEPEDRNIFSYVMEKH
QRNAGANGKILQYMSQMYPYPESLELLVYVSQLLQAEAIRYGVEHFRRNRGRCMGCVYWQ
LNDCWPVASWSSIDYYGRWKALQYFARRFFAPVLLSCEEEGALSSSMNVNEENRRIRKAA
RFCVTNETREPVSGFIKWSIQDAASDICRQGQYSVEVEALSVCSYPWIEFPDIDIRNHYL
SYELWLHGEKVSHGVSLFVPPKHFEFADPKLELRRDGETLLIHAAAFAKGVEIGNEAGDL
LLSDNYFDMDAGEKRVQVLQGSMEGLYVRSMYSLMPDHGTIICRAD

Enzyme Prediction     

No EC number prediction in MGYG000000032_00020.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	4	652	3.3e-97	0.6343085106382979

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	9.77e-102	1	642	9	641	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	4.08e-12	173	421	195	449	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	1.19e-10	187	290	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17786	Mannosidase_ig	2.16e-09	664	743	7	91	Mannosidase Ig/CBM-like domain. This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.
pfam17753	Ig_mannosidase	7.59e-05	748	812	1	77	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL35923.1	0.0	7	811	6	820
QQQ93614.1	0.0	3	814	1	822
ASU28856.1	0.0	3	814	1	822
ANU76049.1	0.0	3	814	1	822
QBE97789.1	0.0	5	814	18	836

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	1.62e-142	4	799	8	816	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482]
2JE8_A	1.71e-142	4	799	10	818	Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A	1.75e-142	4	799	10	818	ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A	4.61e-142	4	799	8	816	Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]
2VQU_A	1.89e-140	4	799	8	816	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0CCA0	1.78e-100	5	801	7	828	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
Q95327	3.78e-100	7	634	25	692	Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
Q29444	1.97e-99	7	634	25	692	Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
Q4FZV0	2.88e-98	7	641	25	700	Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1
Q4WAH4	7.19e-98	26	805	32	834	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000032_00020.