CAZyme Information: MGYG000003277_01842

Basic Information

• Species: Duncaniella sp900762315
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900762315
• CAZyme ID: MGYG000003277_01842
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601		64666.43	4.8808

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003277	3767547	MAG	United States	North America

• Gene Location: Start: 72520; End: 74325 Strand: -

Full Sequence      

MMKTITIMNATLSRLILIMLGIICMSACSSDDNPSGGDVDFIVPENIINNGVVVAKSGGE
AAPFNIKASSAPIAEISATWCKAVIEPTSSATIFRCTVSADANPDAADREAKLTIKQGAH
SVEVPVRQTAADAVIVENTLIDNVPAAGGAIQVKLKANGDVTCTVNDSWITSSRAAMKDM
AFDFTVSENRATVERTGSITFTLGDIVETVTVKQLAGAGAATGDITSSDPREVAAALGLG
WNLGNQFDAHNSGVASETAWGNPRASQKLFDAVAASGIRTVRIPVTWLGQFGSAPDYAIK
KDYLDRVAEVVGYAENAGLNAIINIHHDGADGAHWLDIKGAANDAAKNAEVKKQITAIWT
QIAERFKDKGPWLIFESFNEIHDGGWGWGANRNDGGKQYRTLNEWNQTFVDAVRATGGNN
ATRYVAVPGYVTNPELTMENLVLPTDRAQKTIVAVHFYDPNEYTLNAKFSEWGHTGKDKE
SWGDEQNVRDVFSKLKAKYVDNGIPVYIGEMGNVNRSTDRARKFRLYYMEYVAKAACDNG
LAPIIWDNGAQSAGRECSGLFNRTTGNFYDDGGDVISVMVKALTTDSPDYTLDTVYNSAP
K

Enzyme Prediction     

EC	3.2.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	256	549	7.5e-94	0.9927536231884058

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	2.43e-53	245	550	4	270	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	8.95e-23	227	550	41	361	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	7.98e-14	143	214	10	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	6.90e-10	48	128	4	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004	BACON	7.39e-06	73	128	4	60	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT88430.1	2.16e-222	8	601	1	598
ADY35478.1	5.27e-204	8	601	1	592
ALJ60576.1	1.84e-189	132	601	34	512
AIF26005.1	5.46e-163	225	601	25	402
QRX62664.1	6.35e-159	143	601	46	513

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WQY_A	6.10e-159	225	585	19	384	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]
4YHE_A	1.59e-130	237	601	14	386	NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
4YHG_A	1.27e-129	237	601	14	386	NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
2JEP_A	4.78e-72	226	564	31	377	Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]
3NDY_A	2.26e-66	231	583	13	341	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O08342	1.81e-68	220	563	30	381	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P28623	5.10e-64	207	583	15	372	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P28621	2.42e-62	224	563	39	356	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P23660	1.48e-57	220	571	17	353	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
Q12647	5.67e-54	231	565	26	347	Endoglucanase B OS=Neocallimastix patriciarum OX=4758 GN=CELB PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000011	0.000316	0.999745	0.000002	0.000001	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003277_01842.