CAZyme Information: MGYG000000211_04256

Basic Information

• Species: Bacteroides sp900556215
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900556215
• CAZyme ID: MGYG000000211_04256
• CAZy Family: GH2
• CAZyme Description: Exo-beta-D-glucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
865	MGYG000000211_10|CGC2	100885.44	6.9588

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000211	6486320	Isolate	China	Asia

• Gene Location: Start: 97900; End: 100497 Strand: +

Full Sequence      

MKKPNLNLKRASLLTSSLLCSALLIAVPLRKELNEDWKFKQARLNNWYPATVPGVVHTDL
MDNKIIEDPFFRLNERSMQWIDKEDWIYQTTFRLTPEMMEKQNIELVFKGLDTYADVYLN
DKKILEANNMFREWRTNIKPNLESGENILKIYFHSPIKVDIPKWDALPYQYEAGNDQSEN
GGVFNKKVGVFARKAGYHYGWDWGPRLVTSGIWRPVYVEAWDDARLNDVFIRQQEVNKNR
ATILGEIEILADKEIDKAIISITEASSGKVLAGQVVSLKKGMNKVSLPLSIRNPKLWWSN
GLGEQYLYDFRTDLTIDNRTADTQTKKVGLRSLKIINQPDKDGKTFYVELNGVPIFAKGA
NYIPQDNFLPRVTREQYEKTILDAANVHMNMLRIWGGGIYEEDVFYELCDRYGILVWQDF
MFACSLYPAEGELLENIRQEAIYNVKRLRNHACVALWCGNNECNDAWFNWGWQKRYKKQN
PEYEQIIWKQFNDQYNVTLPQVVKEYAPESFYWPSSPFARYDGGSDDHNGDRHYWEVWHG
KKPIEMYNKERSRFFSEYGFQSFPEFESVKRYAPREEDWNIYSEVMMSHQRGGAHANELI
ETYLLNEYRKPKDFEAFLYMNHVLQGDAIKTAIEAHRRDMPYCMGTLFWQHNDCWPVASW
ASRDYYGRWKAQHYFTRKAYRDILVSPIADESGILKVQVVSDRLKSCSGKLEVNVIKLTG
EVLNQYSRNVKIDANSSRTLFSVPLEEALNGTRKEDVFIHAVLSTNKGKNDYANNYFLVK
QKEVNYPHAMITKSIQPIEDGFEVTLNSDNFARAVFIATGDVNSSFSDNYFDILPRSSVK
VKIHTSLPQNVLEKQLKIVSLSDEY

Enzyme Prediction     

EC	3.2.1.25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	30	829	1.1e-107	0.7845744680851063

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	1.60e-117	30	705	12	655	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam17786	Mannosidase_ig	1.74e-19	693	783	1	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	1.99e-17	791	863	4	78	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
PRK10150	PRK10150	5.50e-17	30	462	12	417	beta-D-glucuronidase; Provisional
PRK10340	ebgA	2.45e-12	87	464	112	455	cryptic beta-D-galactosidase subunit alpha; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO68488.1	0.0	1	865	1	865
QUT88714.1	0.0	1	865	1	865
ALJ60279.1	0.0	1	865	1	865
QUT74423.1	0.0	1	865	1	864
QBJ17295.1	0.0	31	865	13	845

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	1.13e-235	33	865	11	838	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	1.20e-235	33	865	13	840	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	1.24e-235	33	865	13	840	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	3.29e-235	33	865	11	838	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	1.44e-233	33	865	11	838	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
Q5B7W2	3.98e-134	33	750	9	738	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
A2QYN2	1.13e-133	33	742	9	730	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1
A1CGA8	1.32e-131	25	685	1	658	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
Q0CCA0	1.75e-131	30	685	6	656	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
B8NW36	3.76e-130	33	685	9	658	Beta-mannosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 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
0.698083	0.247502	0.048065	0.001041	0.000717	0.004582

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000211_04256.