CAZyme Information: MGYG000000149_01267

Basic Information

• Species: Clostridium saudiense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium saudiense
• CAZyme ID: MGYG000000149_01267
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
823	MGYG000000149_10|CGC3	96820.93	5.0882

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000149	3780856	Isolate	United Kingdom	Europe

• Gene Location: Start: 85365; End: 87836 Strand: +

Full Sequence      

MREKSLNGKWKMRQVGSKEWLEANVPGSVYADLIENEKMEDPYYRDNELNALKLMEYDYE
YLTTFDIDEDILLCEKVLIRFHGLDTLADIFLNNNFIASVNNMHRTWEFNIKRYLRTNNN
EIYIIFHSPTKFIKEAYEKNPLNGSSDAMNGFPHIRKAHCMFGWDWGPRLPDAGIWRSLG
ILGVNEGRIDNVYISQNHKEKKVSLNFKVDIKINDKSNTLRFGVDKEISDYDFRYKVTIT
SPDNEIIVYNDSINEIIIDNPKLWWPNGYGDQNLYNILIELIKDDVVIDKWENKIGLRTL
TISREKDDYGESFAHVVNGVKIFAMGADYIPEDNILAYVNKERTYNLLKQCKDVNFNIIR
VWGGGNYPYDDFFNICDELGLMVWQDFMFACAVYELNDEFEENITNEFIDNIRRIRHHAC
LALWCGNNEMEMFMDNNLWTSEKRLKADYIKLYEYIIPKLLNKEDPQTFYWPASPSSGGS
FDNPNDDKRGDVHYWDVWHGNKPITEYRKFLFRYVSEFGFQSFPSLKSVEMFTEPEDRNI
FSYIMEKHQRNATANGKIMNYMEQTFLYPTNFDTLLYASQLLQAEAIRYGVEHFRRNRGI
CMGAIIWQLNDCWPVASWSSIDYYGRWKALHYYAKRFFAPLMLSCDEEGILTQDINPNPE
PFEVKKSIHLCISNESMYDEVVIVNWKHRKNTGEIIKEKSYKVEIKKLSSVWLEKITLPE
LSLYDEYISYEMIKDNKVISSGTTIFCAPKHFKFINPNLNISVNGDEITILSDSYARSIE
VINEEDNLLLEDNYFDINSGIHKVKIIKGEPKGLKVRSVYDIR

Enzyme Prediction     

No EC number prediction in MGYG000000149_01267.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	773	5e-101	0.7686170212765957

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	4.68e-97	1	711	10	711	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam00703	Glyco_hydro_2	5.63e-16	188	298	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
PRK10150	PRK10150	8.82e-07	210	429	186	417	beta-D-glucuronidase; Provisional
pfam17786	Mannosidase_ig	1.26e-06	668	751	3	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	4.17e-04	756	821	1	78	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
AEF82182.1	0.0	6	823	6	816
ADL35923.1	0.0	6	819	6	820
QBE97789.1	0.0	1	823	15	837
QIB54534.1	0.0	1	823	1	823
QMW79049.1	0.0	1	823	1	823

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	9.13e-153	10	821	15	836	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	9.65e-153	10	821	17	838	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	9.92e-153	10	821	17	838	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	2.61e-152	10	821	15	836	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	1.09e-150	10	821	15	836	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	3.68e-108	3	809	6	828	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
A1CGA8	5.72e-106	25	648	32	663	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
B8NW36	1.09e-105	25	648	32	663	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
Q2TXB7	1.52e-105	25	648	32	663	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
A2QYN2	1.52e-105	14	648	20	663	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000149_01267.