CAZyme Information: MGYG000003916_00188

Basic Information

• Species: UMGS1474 sp900547105
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1474; UMGS1474 sp900547105
• CAZyme ID: MGYG000003916_00188
• CAZy Family: PL8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2020	MGYG000003916_1|CGC3	220465.62	4.6051

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003916	2239460	MAG	China	Asia

• Gene Location: Start: 206182; End: 212244 Strand: +

Full Sequence      

MKRYIRKGLAVLGMVAMLMTMLPTGILLASAEDAADFDLPEGYTLSAIETVDDLKAVHTG
KEASKVYYYLTGNISIDEAEWKPLGTNENTDAFWDILDGNGYAIRFSGADGQGVKATGTW
NASLLFAMNGDALVKNLTVEGSITSSAQSTGAIVGQMVNGTIDRCVNRASVTATNKEGVG
GLAGRVKHGVIVNCMNYGTITGGGFTGGLVGKVSYSEKGVNAVSIANSANFGAVNGKDKV
GGIIGLATADLTYTIENCYNAGTVAGSTLLTQGAIVCSAWPGAVKTVHCYALEDSCTKFL
NTTVKMSAGDMQSQAFADTLNANVEAGIMFADNVNQTEKAVPAVNWQYTENKYPTIPMVK
PVVPQKDLTPEEQMDLIRQRITQYFLRNDAVHSSGAHNGICYVSKAGEYLDMQNEDGSWS
DVDYYCTLSAANGAAWEPYLALDRMLAMSYAWAKEGGEYYHSQKMADGVNKAFDYWASIK
DANPNDPNWVGPWSTNWWENSNGVPRRFGPIGVVMKEGLSKESMALILRRVNKDGSADSG
QNALWNTQNALYWSLAAGDAAQLKKVVEKNLAVNLRVGGLTDEAIQVDNTFHCHGYQLYT
NGYGKSLFSDMSLWIDLLAGTDYAMPQSVLDLMADYMLGGTRWMMRGNLLEMADGYKGGS
ASGYIESLQRMVKNDPKHAAEYQKVLDSITGASSTYNGANGSNYMWTSALMSHMREGYGV
NVRMNSKGMKSTEWRATWPKTDFGNLIFWTADATASVMIDGDEYNSVYNTYDWRHVPGVT
APFVLATHYGFDNDSNDCWGVTNGTYGATAYTFNKHDGTNKRTWGKIGYFFFDNEYVALG
AGIGANHAASIHTTLNQAKAADVSVNGEAVADGTDDKTVQANYVYNNKIGYVFPQSTEVH
LSNLNHTAKKYPTVRGNGYGNLDEDRFGETDVNTFSLWLDHGVAPSNDTYAYIVVPNTTE
QQLASYSANSQIVIVANTDKVQAVRHDGLKLTQINFYEAGTLEYADGKTVSVDGPCSLII
DESGSEPMISQAVSNTKPNTLVNVVLTTDNTNLVTEFCSLSEPYAGKSITQSVGGSSLMQ
SSTTVPEHNAAKVFDKNLETYWESGEQPSWIQYDMREDLYVNNLTVYWGENYATKYELQY
SEDGVSWQTAYTQESGTGGTETIPFNVISRYWRLWFTESSGDVYQIREINFQTSHNLATN
KPMTASAETKPASYAVDGDMSTRWVAERGKQDSWIVADLGMNTRIDGVRILWEASYATQY
NIDVSDDGETWKTVAPVQYKDETGDKIITVQTALPQGTTGRYLRVQGKELALKQYGLSIW
ELEIYGSMQIDSDNAALNKSVTDKAGNTVSQVTDGKTDTLWTSDQSEESLTVDLGEPHQI
DRVEVVWGEPYATAYTWQLSADGQTWSDAATVTQGAGKTESADLSLNARYVRLVMHHSSG
DGYAVAEWNVYGSAISQMNPDKTALKQAIDTRVRDDVYTQESYTAYQNALAIATNVYAST
KATKAMVDEAARNLLDAIDRLEFRHFGTVLATIADQTATKTKQTDILSLNWTNLSQQLDL
SKEDLSKVYLFATLDITRDPNEEVSGLLNNGQIRLRATDENGKERSVYVNTRTLDLHLGS
NVLYFPLSDMVVANADNGMDWSTVNRFRMYIDSVNKFDGAMTMALNDAKIIRTTEPTKVK
VACVGDSITYGVGASSSSQNYVSQLQKRLGSHYTVQNFGNSGKTLISGSADGNDYVKTDT
YKNSLAFEPDVVTIMLGTNDSKDQNWKSPYKEKYEQDLRDLINAYRALPSHPVVILATSP
TAYSRNWSINDEVITGEIAPLQRKVAAEMGCTLIDANSGTRGLDGSVYFADGIHPSDTGH
ALLAELFEKGVREAGARLYGFAVNGQQAVIDDAAGSVSLTLPYDTDLSQLKPELTLMTSA
TVAPLDVTNYTKPVTLTVTAPDQSTTRVYTVTITREQPVYTLGDVNADQQVTIIDALMTL
QAAAGKIALTNTQNLAADMNKDGKVTAADALVILRLATGC

Enzyme Prediction     

No EC number prediction in MGYG000003916_00188.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL8	704	957	1.7e-43	0.9839357429718876
CBM32	1205	1323	2.4e-25	0.8951612903225806
CBM32	1080	1189	5e-21	0.9112903225806451
CBM32	1342	1447	5.2e-19	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01083	GAG_Lyase	1.64e-83	436	1035	61	692	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.
cd01827	sialate_O-acetylesterase_like1	2.26e-53	1679	1865	1	181	sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
pfam02278	Lyase_8	2.65e-45	704	959	3	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.
pfam13472	Lipase_GDSL_2	6.47e-27	1683	1862	1	176	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229	SGNH_hydrolase	2.85e-24	1681	1869	1	186	SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW73769.1	2.41e-260	371	1479	30	1146
QPS12968.1	2.41e-260	371	1479	30	1146
QQV04833.1	6.55e-260	371	1479	30	1146
QQY28197.1	9.14e-260	371	1479	30	1146
QUN12787.1	3.28e-237	377	1478	36	1150

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CB8_A	2.38e-54	406	1054	28	661	CHONDROITINASEAC LYASE FROM FLAVOBACTERIUM HEPARINUM [Pedobacter heparinus]
1HM2_A	3.35e-54	406	1054	50	683	ACTIVESITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS [Pedobacter heparinus],1HM3_A Active Site Of Chondroitinase Ac Lyase Revealed By The Structure Of Enzyme-Oligosaccharide Complexes And Mutagenesis [Pedobacter heparinus],1HMU_A ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS [Pedobacter heparinus],1HMW_A Active Site Of Chondroitinase Ac Lyase Revealed By The Structure Of Enzyme-oligosaccharide Complexes And Mutagenesis [Pedobacter heparinus]
2E24_A	1.06e-23	413	1039	37	701	ChainA, Xanthan lyase [Bacillus sp. GL1]
2E22_A	1.40e-23	413	1039	37	701	Crystalstructure of xanthan lyase in complex with mannose [Bacillus sp. GL1]
1J0M_A	5.53e-23	413	1039	37	701	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q59288	1.84e-53	406	1054	50	683	Chondroitinase-AC OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=cslA PE=1 SV=1
D5EV35	1.73e-31	1666	1872	261	480	Acetylxylan esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axeA1 PE=1 SV=1
Q9AQS0	1.03e-22	413	1039	62	726	Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly 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
0.000748	0.998254	0.000254	0.000268	0.000222	0.000209

TMHMM  Annotations     

start	end
9	31