CAZyme Information: MGYG000004085_01885

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UMGS1253; UMGS1253
• CAZyme ID: MGYG000004085_01885
• CAZy Family: PL8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2215	MGYG000004085_14|CGC1	242963.35	4.2205

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004085	2144710	MAG	United Kingdom	Europe

• Gene Location: Start: 10686; End: 17333 Strand: +

Full Sequence      

MCILTRIQRFEKGDRIMCKKLLAALVCVTMLLSVFSTLAALAEPVDDFAALRSRWDEYLT
GGDSYDLSDEKIKAQVDSITETAQTEWDSMNKTEPELGYLWEDVNDWSTSHTIADTATRL
YHLALAYSTHGSTLEGNAELLDDIEYGLTWLNENKYSTTIKPYDNWYDWEIGIPGTLCNV
LILLYDDMDPALRDSLVAAMLKYSPDPAKFNYVGTKGNPSSGANRVWLSMNHCLIGVITN
DADKLTYGRETLDTVLTYVDYENAGKETVGDGFYDDGSFIQHTRFAYNGGYGLSLITEVA
DAIYLLGGTQWELMNGSNVYQWIYDSYEPFMYKGALMDMVSAREPARYYRTDHTAGKKFM
TTLTVLAQNAPEEHKTAFESMIKLWASEDTTSDFLSGMSIYTLQKAQDIMENATPAEPWR
GYKQFAAMDRAVYHGEDYAVGLAMYSYDRTHSYEITNSENKRGYYTAAGALYLYNDDLKQ
YSEDYWATANWFRTPGTTCFTDTGIKENSKSNNFAGGTDMDDMYGVSGMIYTPRGAENTL
TGLEARKSYFMFDDEVVALGTAGSELDKGVETIVENRRLTGEGTNTFTVNGEQVLTDAPK
EWAPWNPYTAQYAHLTGNVEGADIGYYFPGGANIQASRYIRTGNWKDINDKYYTTDEKSG
NYLGIRFNHGAKPALGEDTYAYALLPNMTEEETKAYNDNPDIAVIKNDDKAQAVKEKTLN
MTGAVFFTDSDAVAGPLQSNKKAAVMIKEGTDGLLDVSVSDPTWDNDGTIELIINAPYVS
TESADSTITAAAEGDKTKLTINVAGQHGSAQKAQIKVGGTLTNLPEIEEPKPEPEPEPEI
VPDVKIINDDFNDLAIGANGKQVSASSRGKGWTSQQFFSNDRKFIQYDPHDATKTDKVAM
VLIPKEDVGNKISTSSAFKIGARGNAWIAQFRLMFNAPPVADGELAPISPADAAENGNNF
YLRVRNSSKNMFYLAKFDGGERKVGLGSKSTLSGETAQFDAGTWVDVTAVCNIDPTDRSS
GKMTLYLYAPGAVTDNQDNDTKKDYVVIEQEFTPPSFLGASANEQAPFYLEIGKSCPREM
NWWLDDINMYEPNSFISSMEETADVSTTGPVEVTFNHTADVRTLVKENVSFVDAEGETVG
ASKVEFDPDDLSKITITPEKELKGNTEYTLDLSKVTDWVGTGALAVTFTSGEATGTDPNP
GPEPEIVPDVNEIVDDAQSYNIGTKGSKFDKDKGWGTVSDSFSVREDFDAVGAALGNKAF
RVKAPDPEKDANITTRATRNNGLPMVISGRIMAEKLENGSNFNLRVGDAKSSNTQYLMRI
QGSSLEVATNTKSTMPDDSYKIKPGVWVRYTAYYGAKQNRVILYMTGGITDKDGKDVPYM
IQEVNATPPSAVTNATGGRGPEFYVNFKAGAEGSFWLDDINSYTPNSFISSMEQATDVPT
GGPITVNFNHEADVRTLTAENVTFRAADGSTVAAQSVEVDYSNLNKLVITPAAALAGFTE
YTLDLSGVKDWNGTSCLSTTFTTGIGGGVELVPIETLSIETLTDNLIQSEGKTAPVVFKA
TATPLNVDLNTIEWYVNSQLQTGVQGVNFTYTPEAAGSYVVTAKANGTAVMSNAITITVS
EEEIIPITEIKLDPGEITVWADFGLPIEPKVTITPSDATNKALTWHSDNTEVATVDENGN
VTPVAPGTAHITATAQDAGGTVSNTFTINVTPAQNRADDQKLNLDPVSGKNTRIDINEYL
AWPENVGEGQIALWSGNATGAISLTVDDSLEYDFDQWKKWKEEYGFPATFFVPTKPGYIE
EFDLWQDLVNNGMDVQSHTYGHLDSDQISALSSAQSIYEFSKPLEELDKLEGGDKAHTLA
YSYGGGDENYARKFYIAARGTQGKLNKADNVNYNRVSGVSMKNTLPLLATEDRNTSSKWS
LEAAVKTLYDPSGEYRQYGVSYYGGWFVMYSHGLSTNKSPNSDLKNLYLKEHPNAPTDED
GNILDEEGNKVDFSLRAVFSYMFENWIGPAVENGDIWLDTFTNVAKYGQERDTSKLEITN
NTDSITYTLTDEMDDTLFTFPLTVKIKVDSSWENIEAVQDGKKLPIKTVDVDGSRYVLVE
TVPDTGAVTVAPGQGGEESADISIMDGVSVTHDNGAITFNSTADMDVTVYAAVLTTDEEG
YEQLKQVKTYDASLKADTEQTVEVELPVAQASGEKAVLMIWENGTLKPITKQIEL

Enzyme Prediction     

EC	4.2.2.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL8	423	690	5.4e-70	0.9884169884169884

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	0.0	47	762	1	693	Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.
pfam08124	Lyase_8_N	1.48e-82	55	383	1	322	Polysaccharide lyase family 8, N terminal alpha-helical domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.
pfam02278	Lyase_8	5.13e-70	423	689	2	252	Polysaccharide lyase family 8, super-sandwich domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.
cd10970	CE4_DAC_u1_6s	4.08e-15	1760	1967	1	188	Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 6-stranded beta/alpha barrel. This family contains uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.
cd10967	CE4_GLA_like_6s	6.97e-15	1760	1964	1	189	Putative catalytic NodB homology domain of gellan lyase and similar proteins. This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAG24953.1	1.21e-170	26	822	15	794
ALC80364.1	2.77e-167	40	813	31	782
AXR85425.1	2.01e-165	14	820	7	785
AAG42262.1	2.92e-162	28	815	16	784
QYR20590.1	8.46e-161	39	929	26	882

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F2P_A	1.47e-165	46	820	4	754	Structureof Paenibacillus xanthan lyase to 2.6 A resolution [Paenibacillus]
2E22_A	2.73e-160	46	818	2	752	Crystalstructure of xanthan lyase in complex with mannose [Bacillus sp. GL1]
2E24_A	7.08e-160	46	818	2	752	ChainA, Xanthan lyase [Bacillus sp. GL1]
1J0M_A	7.08e-160	46	818	2	752	CrystalStructure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1],1J0N_A Crystal Structure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1]
1X1H_A	3.48e-159	46	818	2	752	ChainA, xanthan lyase [Bacillus sp. GL1],1X1I_A Chain A, xanthan lyase [Bacillus sp. GL1],1X1J_A Chain A, xanthan lyase [Bacillus sp. GL1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9AQS0	7.51e-158	41	831	22	790	Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly PE=1 SV=1
Q59801	7.31e-71	47	762	48	768	Hyaluronate lyase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=hysA PE=3 SV=1
Q54873	2.26e-64	38	752	281	983	Hyaluronate lyase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0314 PE=1 SV=2
Q53591	7.27e-59	38	752	242	965	Hyaluronate lyase OS=Streptococcus agalactiae serotype III (strain NEM316) OX=211110 GN=hylB PE=1 SV=2
O82833	2.33e-58	1719	2112	1254	1609	Gellan lyase OS=Bacillus sp. OX=1409 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
0.000786	0.998369	0.000267	0.000187	0.000177	0.000171

TMHMM  Annotations     

start	end
21	43