CAZyme Information: MGYG000002257_01779

Basic Information

• Species: UBA737 sp900547305
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737; UBA737 sp900547305
• CAZyme ID: MGYG000002257_01779
• CAZy Family: GH2
• CAZyme Description: Exo-beta-D-glucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
808	MGYG000002257_77|CGC1	91917	4.8222

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002257	2338223	MAG	Peru	South America

• Gene Location: Start: 314; End: 2740 Strand: -

Full Sequence      

MLLNGEWKCILIKAGDVPQTFSAAVPGCIHTDLKRAGVIGDYFYRDNAEKIRWIENCDVT
YQKQFDVDSVENNEYLRFEGLDCYCDIYLNSIKIGSADDMFIPYEFSAENVLRAGTNLLE
VKFRSPIKEVAGRPKRDGAFTTERLYTRREQCTYGWDWVTRFVTMGICGDVSLEKREADS
FDNVYIYTKGITPFAASVAVEAAFRDITGNGFADFEIISPHGETVFSEKRAIFESIIKIT
ADIPNAQLWFPTGYGEQPLYQLKITANGKESITEFGIRKVDILEIDDNFNPEYKAKAEKL
KKNPHLLKNDRNEKTSAFWLVINGVRIFCQGGNWVPCDPFVSEETDEKIKLLVQSAHECG
YNMLRVWGGGVFEKDSFYSECDRLGILVTQDFLMACGTYPEDDKDFLDKVSCETAAAAVR
LRNHPSLVWWSGDNENAVDGYFNKKSFPGKTVVSKSIAPVLSRLDPQRAFLLSSPYGGVP
FKSAACGTTHNTAYLGDWFNFVSGETPFDYYNEINRYLSRFMAEQPSYGLPFVSSLKKFL
TDEDIFGKNSDIMEYHCQNNPCLKETIFAYSEIMAEGFFGKYESPQDRIYKLQLLQCEWL
RVSFELFKRNQWFSSGIIYWMFNDCWPASVSWSVVDYYGNPKPAYYVFRRCAKPVITSLH
EEDGKIKAYVCVNGKNGVSAKGRVYLYNVLTGEENTLAEFDGEFSVGSTCAAAAEKSKIP
QIEQNENIVLCDLESDICSDRSFYCPNYFKNVPWGKNNAFVLTETGSDFEITADTCIPYV
MIDTERKLSDNCFFLKKGETVTLKIGRQ

Enzyme Prediction     

No EC number prediction in MGYG000002257_01779.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	691	1.9e-77	0.651595744680851

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	3.21e-50	3	716	15	687	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam02837	Glyco_hydro_2_N	1.57e-06	3	122	4	132	Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
PRK10340	ebgA	2.12e-06	61	437	113	451	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK10150	PRK10150	0.003	378	468	337	443	beta-D-glucuronidase; Provisional
pfam17753	Ig_mannosidase	0.003	762	805	8	56	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
QJD84958.1	5.07e-167	1	807	5	834
BBI36571.1	2.20e-165	1	807	5	834
ACI19676.1	1.21e-115	3	709	6	686
ACK43074.1	1.21e-115	3	744	6	704
AJS61217.1	5.64e-114	1	805	1	812

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	1.58e-115	3	709	29	709	Crystalstructure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12]
2VJX_A	1.63e-85	1	670	9	669	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	1.69e-85	1	670	11	671	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	1.72e-85	1	670	11	671	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	4.40e-85	1	670	9	669	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q95327	5.19e-81	3	669	25	705	Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
Q29444	2.48e-79	3	669	25	705	Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
O00462	8.00e-77	3	669	25	705	Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3
Q4FZV0	5.27e-71	3	669	25	705	Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1
Q8K2I4	6.43e-70	3	669	25	705	Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 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
1.000077	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002257_01779.