CAZyme Information: MGYG000004088_02242

Basic Information

• Species: Firm-11 sp900548145
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900548145
• CAZyme ID: MGYG000004088_02242
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
849	MGYG000004088_68|CGC1	97950.58	4.9362

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004088	2947168	MAG	United Kingdom	Europe

• Gene Location: Start: 2970; End: 5519 Strand: -

Full Sequence      

MTLFLNGTWKVTHRPYQADIQDILAENFVPEGWLNANVPEEIHATLRRAGAIRGNTYDKR
EDEERWIEEKDWIYCKKFFVPATEKTKSATLLFEGLDTFCEIYLNGEKLGDHQNMHTACR
LEAASRLRWGGQNTLVIRFFSPVAFVAGEDQSEIFSITTSERIFARKAQMNYSWDFCARC
VTVGIWKPVSLIPHKTPEIDNYYLYTDSLKDGQAALGLETELRCFPGVQAEGCTVHACLS
DGETEVWNWEGSPEEAKKVSFTLSQPRLWWPRPYGEAFLYQFRLQLWQNGRCVDERAQRF
GIRTIEVLQERQEDGKSFQFSVNGKPLFLRGANWVPINTVYTDITRRDYEILLHDAAHGN
LSMLRIWGGGIYEDPAFFELCDQHGILVWSDFMLACGIYPQTEAFLSAMAQEADEVLKTY
RNCTSIALWSGDNENGQAYGWAGRPYEFESDRISNQVLKEACARLDPRRYYLPTSPASPD
PDFRGGDNPSSPYQGDLHLYIMSGDPGVTANRDYGKEYYKRVLGFRPRFMSEFGFISLPE
KDSYYRFNVRREPLRNPSEIIRFLPSTKQMLDEGSIEDVIHYSQLFNSMALKFWIEHFRS
LKGVCAGSLYWKFNDPLADCPDVWMYPSHMCAVDMYLRPKMTYYYTRRAYDDVLVMLEEE
SGGWQAVVCNETDRPIEGTLRIEHRTFHGDLLWSREQAVFCGADAAVHLGHVAKDELPVH
DPAAEYLRVILTADGQVYDNRYFFLDVNELHRLVLEPAGLRIVRTARQGDRLRVELRAEH
YARCVRLNILDMRADYSDNYFDLDAGSSRVITIDLQESSEPLFALTLYAEGENVERLCLP
LSDIPEEKL

Enzyme Prediction     

No EC number prediction in MGYG000004088_02242.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	5	671	4.6e-89	0.6303191489361702

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	1.33e-64	5	811	15	782	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10150	PRK10150	3.06e-12	74	469	69	443	beta-D-glucuronidase; Provisional
pfam00703	Glyco_hydro_2	5.98e-12	199	303	3	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17786	Mannosidase_ig	2.08e-08	668	744	7	86	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	1.72e-07	763	818	6	61	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
QNK54904.1	1.51e-121	5	813	11	823
BCU81949.1	2.28e-120	5	823	3	832
AZK48395.1	3.12e-120	33	823	21	829
QZA32915.1	1.75e-119	3	829	1	828
QPC83320.1	2.96e-119	9	813	5	812

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	1.40e-110	33	750	43	752	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	8.33e-94	31	813	23	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	8.67e-94	31	813	25	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	8.84e-94	31	813	25	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	2.27e-93	31	813	23	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0CCA0	4.06e-79	25	664	18	665	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
Q5B7W2	4.69e-76	30	664	23	667	Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2
A1CGA8	1.74e-75	25	682	18	698	Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 SV=1
A1D911	6.23e-75	25	664	18	667	Beta-mannosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=mndB PE=3 SV=1
Q4WAH4	1.18e-74	38	682	32	698	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
1.000086	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004088_02242.