CAZyme Information: MGYG000000174_02078

Basic Information

• Species: Parabacteroides faecis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides faecis
• CAZyme ID: MGYG000000174_02078
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
867	MGYG000000174_4|CGC9	99429.39	5.5882

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000174	6515019	Isolate	China	Asia

• Gene Location: Start: 397601; End: 400204 Strand: -

Full Sequence      

MRYKTVLSAVALAALATTTPALADGVAKQNIDKGWTFKQVRGNNWYPATVPGVVQTDLMD
NKIIEDPFFRLNERSIQWIDKEDWEYKTTLNVSPDIFNKDNIELDFKGLDTYADVYLNDS
CILKADNMFREWTVNVKNLLKKDDNELRVYFHSPIKVDLPKFEALKFPVEAGNDQSENGG
IFDKKVSIFARKAGYHYGWDWGPRIVTSGIWRPVYLVGWNNARIDNIFYDQTNVTAKRAD
IKTRVQVVADKDGEITLNIKADGIKNTWTKKAQVKKGINVIETDLTVNNPKLWWSNGLGE
AHLYPFTATISMDNKVADSNTTNIGIRSIRVINKPDKDGHTFYFELNGVPVFMKGANYIP
QDNFLPRVTAEQYETTVMDAVNANMNMLRVWGGGIYEEDLFYDLCDKHGILVWQDFMFAC
SVYPLTPDLEENIRQEAIDNVIRLRNHPSLAIWCGNNEIHTAWFNWGWMKKFDQYGVTEQ
LHNDTKKLFNGILADVVKEYDPTIFYWPSSPYGGDPDAKCESGKPNWNPNGDAHYWGVWQ
GVDSVAHFNKVKARFFSEYGFQSFPEYQSVLKYAPEERDHDIYSDVMMAHQRGGQIANSR
IENITLEEYRKPKDFPSTLYMSILLQGDAMKTAMEAHRRMMPYNMGSLFWQHNDCWPVAS
WSSRDYYGRWKAQHYFTKKAFRDILVSPIAEDGILNVWVISDRLKAVKGKLDIRVMDLKG
SVLFTKNSNITLPANTSKIQFSAPIESLVAGKNLNEVVVNARFTENGKESEVISNNYFFT
RYKDIDFPKADIQMTSVPAGDGFDVTVQSDVFARAVFLSIDGIDNFFSDNYFDLLPNEPV
TIHVTTELDKDSFDKQLKYQSIVDAYN

Enzyme Prediction     

EC	3.2.1.25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	28	769	1.5e-105	0.7247340425531915

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	6.54e-110	34	847	18	787	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam17786	Mannosidase_ig	7.66e-22	693	784	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	1.17e-20	789	864	1	78	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
pfam00703	Glyco_hydro_2	1.22e-12	222	327	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
PRK10150	PRK10150	1.48e-11	208	458	168	417	beta-D-glucuronidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO68488.1	0.0	28	866	30	865
QUT88714.1	0.0	28	866	30	865
ALJ60279.1	0.0	28	866	30	865
QUT31677.1	0.0	14	866	5	856
QGT72566.1	0.0	14	866	16	867

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	2.47e-232	31	866	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	2.63e-232	31	866	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	2.72e-232	31	866	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	7.21e-232	31	866	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	3.15e-230	31	866	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
A1CGA8	3.25e-122	31	718	9	703	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	9.35e-120	28	845	6	827	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
A2QYN2	7.17e-119	27	860	5	840	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1
Q4WAH4	7.69e-118	31	718	9	703	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
A1D911	1.50e-117	31	718	9	703	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000282	0.998925	0.000214	0.000209	0.000190	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000174_02078.