CAZyme Information: MGYG000003160_00055

Basic Information

• Species: UMGS1858 sp900555705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1858; UMGS1858 sp900555705
• CAZyme ID: MGYG000003160_00055
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1324	MGYG000003160_2|CGC1	145504.57	4.2991

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003160	1773026	MAG	United States	North America

• Gene Location: Start: 17324; End: 21298 Strand: -

Full Sequence      

MWKKWLSGITAAALLAGGVTGVSAAEGSENPLPLRTWYTAAAADWENEATPIGNGFIGGM
VFGGVDNDRIQINEHTLWSGGPGANPNFDGGHKGTAEGARAALQEIRQMLQEMMNEFSEN
HTAYEDEDGKLVTSNYEDTSELKSLLEKLKGTKANFGSYQTLGNLMLTDPSLAEPVLQEA
TSSAEPADLSGEVARNLFDGSSTTKWFAGNSADKDNLTWPVTVTWSYDQAFSTKSYSLIS
GNDTPGRDPKNWKLYGSNDGENYTLIDEQTGVAFADRGETKSFEMEKQVSYSHFKLEILE
TAEHNPPQLAELTLLNANKGATAAYTDYTRSLDLRNAVVTVSYKQDGVTYTREYFVSNPG
NVMVVRLSASEKGKITRQISLTSEQIKSTVTASGDTVSLIGQPADQRADGLHFASQVKVV
PTGGSMTTGTGAVTVTGADEVLLVFSAGTNYVQCMDDSYDYFSDEDPMKAVEANVNAAAA
KKYDALLKAHVDDYSELFSRVELNIGASEMPAKPTNQLLTDYNKINTALEDRYLETLYYQ
FGRYLLIASSREGSLPANLQGIWAEGLNPPWSADYHTNINLQMNYWLAQQTNLAECHLPV
IDYINSLVPRGYESAQHYYCTQDGEDVRGWVIHHENSIWGNTAPGESDAFYFPAAAAWMC
QDIWEYYAFTMDEEFLEENYNTMLEAALFWVDNLWEDERDGKLVSNPSYSPEHGPYSLGA
SCDQTIIWELFEEVVKASEILGKTSTELEEIKAAQAKLSLPEIGLGGQYMEWKDEITLDI
TGDGGHRHVNHLYALHPGTLVVAGRSAAEDAAVEAMKQTLRTRGDGGTGWSKAWKINFWA
RLRDGNHAGVMVNQILLQSTLPNLFDTHAPFQIDGNFGATAGMTEMLLQSQGDSIDLLAA
LPAMWANGSVKGLKARGNFEVDMEWKNQMLQSASVTSEVGGDCTLSYYGLSRAKVVRESD
GKTVAFKADGDVITFATEAGETYRIEEIPQDQKMSNPQSFLRGKFDNLYNKSILQATKLP
EEYGDNGAYLAGFEDASLAEVLGFRPNDVITRYNGTKITDVLHLMKMYEETRDGGKVVLQ
VWRQDRYVKIEFRKGVSDNSRIMPSQIEAEDFDEVKGANIKAESCAEGGYNLSNINGGDW
VVYKNVYFPVPPDGVLFRVAKEDGDTTRIDVRLDSPTAPPIGSIDIVGTGGWQIYSTKVL
DINATEEAAGIHDLYFTFSSSVNINYFYVSSGEKTIAEEVPYGPGDPDEPITPDDGELGD
INGDGVVNTTDARLALQYAVEKITLNENQLKAGDVDGNGVVNTTDARLILQYAVEKIDRF
PAEK

Enzyme Prediction     

EC	3.2.1.63

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	303	949	3.9e-234	0.8628808864265928
CBM6	1108	1229	2.6e-24	0.855072463768116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	6.44e-44	37	453	2	233	Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
cd04084	CBM6_xylanase-like	1.15e-30	1105	1227	1	121	Carbohydrate Binding Module 6 (CBM6); many are appended to glycoside hydrolase (GH) family 11 and GH43 xylanase domains. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family domains, including GH3, GH11, and GH43 domains. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB6s belonging to this family are Microbispora bispora GghA, a 1,4-beta-D-glucan glucohydrolase (GH3); Clostridium thermocellum xylanase U (GH11), and Penicillium purpurogenum ABF3, a bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (GH43). GH3 comprises enzymes with activities including beta-glucosidase (hydrolyzes beta-galactosidase) and beta-xylosidase (hydrolyzes 1,4-beta-D-xylosidase). GH11 family comprises enzymes with xylanase (endo-1,4-beta-xylanase) activity which catalyze the hydrolysis of beta-1,4 bonds of xylan, the major component of hemicelluloses, to generate xylooligosaccharides and xylose. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold.
smart00606	CBD_IV	3.66e-26	1104	1227	5	127	Cellulose Binding Domain Type IV.
pfam03422	CBM_6	2.14e-24	1108	1231	1	125	Carbohydrate binding module (family 6).
cd14256	Dockerin_I	1.38e-17	1258	1312	1	55	Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQA09897.1	0.0	19	988	18	1016
QUT72093.1	0.0	19	988	18	1016
QUT39630.1	0.0	19	988	18	1016
BCA51189.1	0.0	19	988	35	1033
QMW88739.1	0.0	18	988	20	1016

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KMQ_A	9.64e-123	326	949	150	761	ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
4UFC_A	3.22e-117	330	962	134	758	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2RDY_A	8.56e-113	328	983	112	787	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAB_A	2.82e-110	326	985	154	894	Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAD_A	1.94e-109	326	985	154	894	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	1.33e-106	328	969	163	834	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	1.45e-96	309	927	121	758	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	1.83e-86	324	925	138	775	Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
Q2USL3	1.25e-69	326	936	129	706	Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2
P10478	7.88e-15	1105	1271	299	441	Endo-1,4-beta-xylanase Z OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xynZ PE=1 SV=3

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
0.000463	0.998663	0.000255	0.000230	0.000207	0.000180

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003160_00055.