CAZyme Information: MGYG000000148_01744

Basic Information

• Species: Faecalimonas phoceensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Faecalimonas; Faecalimonas phoceensis
• CAZyme ID: MGYG000000148_01744
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1629		181032.98	4.3608

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000148	2855435	Isolate	United Kingdom	Europe

• Gene Location: Start: 30327; End: 35216 Strand: +

Full Sequence      

MKKKGTWMRASAGALSAAMVLGSVTVAPAVKAENVEEKAGYEVNYALNSKVTASNQELAN
QWGPEKAVDGIVNRDAEKPEQSRWSTAQSTTQEARTLTLDLGAVKTFSQFVIEWERTNIT
NFKISVSDTEDGTYKDVYVKEDGKNITSLTSRINLEKAATGRFVRLTVNGYTLNPGNWQS
VSLYEFKVLGEAENLSEGATVAADGYEDNLEKFQPSKVVDGDDTTRWASPAKLGQHWISL
DYGKEISIQSFKIHWERTNATKYRLEKSSDGTNWEPVVSFEKKPDSYQQIINLDEPIDTQ
HVRLFIEEFDPKGAPENGAEVTWNTVGIWEFETYAGKLEEPENTQDPQEVADNLELPESI
EGDSKKFTMPEVPEGFEISFVGADYEQILDRDLTVYQPLVTQQIKMNFNVKAEGKDGKAV
DSKEYTMTVTGKYEQEEGDNAKPAVIPELAEWKGAKGGEFAVKDGSRIVVANKDKAALQR
AATEFQKDYKDLFGKDLEIVYADSANAGDFFFTLVEAGTGLKEEGYNLKIGDSVTVEAET
STGAYWATRSILQILKQTDGTIAKGEARDYPKYEVRGFMLDVGRRPFSKKIVNEVAKTMA
WYKMNDLQLHLNDNYIFLEDYTTAGEDPMTAYEGFRLESDIKADGNLNKADLTSDDMYWT
KDEMRQMIQDYREIGMDIVPEFDTPAHSLAFTKVRPDLKMGGNGRENDHFNLATPSGGDA
SETPYAKSLEFVEGLWDEYLEGENPVFDEETIVNIGTDEYSETYKEQFRQFTDDLLAHVQ
EKGNQVRLWGSLTARKGQTDVRSEDVQMNIWNDGWANPKEMYKEGYDLIDMNDGTVYIVP
AAGYYGDYLNKQHLYSNYDPAKRMGVPVGSEQTLGGAYAIWNDMVDKKANGLSEMEIYDR
FNDAAPFYASSLWGDEEKTYAEATEVSEAVGEAPRTNAYDKVDSKGDTIVSYDFDEGLND
ESGNGYDAKDAVNAKVEDKAFVLNGKESYVSTPLDRVGPGKELSFDITMKKPGMPGEILF
EADAEYGTYDIRIMEDGTLGFTREGYDYSFGYKLPVNQKVSLTIRTDGDVTSLIADGKKY
TATGSYTYEGDLKASNISRASLSLPTERIGSKTNAVNAVIDNIVLTSKVVKEDLTEGAID
SKDFTVTADNENSDGKITNAFDNNISTIWHTQWSPNKKPLPAVITIDMKKNYDINGFYYM
PRQTGNNGYILEYTLEYQDASGNWKKAVDKGTWSSNGSEKNVRFKPINTSKLRLTVTKGQ
NDFGSAAEFKVLGGTEDLTKVPLRISTYVEGRGTAEVSKEQIIKGEEVTFTAKADKGNKF
VGWYDIFGNEVSKEASYKVTPEDNLTLVAKFEESDTPVDPDGVNKGSLKKLYDDCVAADR
DEKEYTPGTWKAYADAMDAAKAVIDDKEATEEQVKKAHDDLQKALFELRLIPNKDKLEDL
IKEAEKMDLSGYTSESVKVFEDALAQAKVVMEDPEADQDAVDAAEGQLAAAVEQLEKADK
PVVPSEVDKSALEKYYNECVSYYKEADYTADSWKVYKEALTNAKTVLDDEDATAEEIKAA
TEKLAKAAKDLAKKEENKKPSTPSAGGSDESGKKPVTGDSTAAPMMMVLAAAASVIAGKE
ILKKKKMDE

Enzyme Prediction     

No EC number prediction in MGYG000000148_01744.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	568	913	1.1e-54	0.9673590504451038
CBM32	211	332	1.1e-22	0.8709677419354839
CBM32	51	187	2.8e-19	0.9435483870967742
CBM32	1149	1270	8.3e-19	0.9032258064516129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	2.98e-115	574	915	1	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd02742	GH20_hexosaminidase	5.36e-30	576	890	2	285	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
pfam02838	Glyco_hydro_20b	5.36e-27	442	569	1	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
pfam00728	Glyco_hydro_20	1.95e-25	573	890	1	326	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	8.04e-21	516	837	198	534	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPS14026.1	0.0	42	1583	42	1482
QMW75640.1	0.0	42	1583	42	1482
QQV05894.1	0.0	42	1583	42	1482
QQY27155.1	0.0	42	1583	42	1482
QTU82680.1	6.05e-315	37	1281	28	1247

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.74e-115	348	1078	1	679	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	2.59e-25	442	915	33	476	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
6YXZ_JJJ	7.12e-18	194	845	20	608	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6Z14_JJJ	1.23e-17	194	845	20	608	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
4A41_A	7.33e-17	1138	1271	24	159	CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.52e-121	345	1078	20	701	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
B2UQG6	5.17e-16	460	885	48	478	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
Q9HGI3	9.71e-15	523	860	128	471	Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA PE=1 SV=1
D4AYT4	1.74e-14	523	918	139	563	Probable beta-hexosaminidase ARB_01353 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_01353 PE=1 SV=1
E9DFH0	5.39e-12	523	881	121	484	Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 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
0.000247	0.999082	0.000160	0.000190	0.000166	0.000140

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000148_01744.