CAZyme Information: MGYG000001697_01451

Basic Information

• Species: Erysipelatoclostridium saccharogumia
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium saccharogumia
• CAZyme ID: MGYG000001697_01451
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1673	MGYG000001697_24|CGC3	187232.08	4.1527

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001697	3141483	Isolate	Germany	Europe

• Gene Location: Start: 35605; End: 40626 Strand: -

Full Sequence      

MLSCFSQKIVLVNAAEEYENIALNKPVITSSVRPARSELVGALAVDGIDDDESSRWSSKM
ATGLGENEGPSEDGTVEQWITVDLQNVYDLLRIYISWEGAYAKSYQIQTSLDGNNFTDLY
VNTDAKGGKQTIEKDAFISDASARYVRIKCNEPVKASWGYSIYEIEINGAQKDNVNLALS
KDVSYSGVEGGKVGDSWKYPQFVGEKVVDGDETTRWSADKTDDQWIIVDLKEVEILSQVN
VNFFREPLEYTVEISKDGNDYTTILDVKDNSMINVENMREIAFDPQEVRYIKVNQTKMFT
NPSNNNKYGGSIFEIEAYRYAMLEPEIETAKMALTKLESEGFELPENSNEKIIFSEAITK
NFDVEIYGSDYQSIISLDGIYYQPLVDKDVHIMYKVTNKNDENDIAISSNDNKIHIPGKY
EDSGKNEFPNVIPSIQEWHSENGNYSISKDSKIIYNDESLEVQANILSGYLNKLVGLDID
VKKGTNPEDGDIYLSLTDEDDVAILGDEGYIMTVDDYVTIDSTTLNGVFYGGVTIVQALY
LNLDELTIPKGTAHDYPKYEVRSIALDIARSEIKLDYIKEITEMLPLFKVNEIVMHINDD
RGDKITNSEIGSEENIQQAKELSSFRIENDKNIGSHSYQISKEDYIEYQLEAAKYGVSVV
TELDTPAHSAVFSLLPEMHDNMYDVRHLKILDDSSTDVNNVTLHQPTIDFVDELTQELIG
NAPGDAVIQTPIFHFGTDEYNSAPIYSEAMQQYINHYTEYIQDRGYEARAWASSDGSSGF
KGYVTPQNKEVTYYLWAPYWADVKKTVANGNPIINCSGSWLYIVPGGNNNYNNYLNIEKL
YNQWSVNDITTTRGSGGAVLPISHPQLRGASVVLWNDDGFLLDGVSDFDIFDRLKYGIAL
IGERTWYGEKTEDQSYDEFKTSYEYLLKTGPSATSNPARYVQSKTETVVDIDFETINDNK
AIDVSGNDYNGILNSTTARGISGNALVLDGDSYLQMPFDSIGFPATVSFDIYIDENTSKD
AALFEGNDGKINLNQKNKAGEYTGKLGYERDGYTYVFDYEVETEKWLKIMITADKDGTNL
YVNDKLISAGKRTEFGSYVTKNLSTSMILPTEKIGSGIIGKLDNFKIVNEKIEIAGPENI
ASTAIDAVASNVYNENFTGIKAIDGSLLTRWATTNDITSATLELTFDEEVSVNQTRIVEY
KAAYNYITSYNIEYWNGENWVVGHTYNVDNSEKMAVAGVTNGYEFGSQFDTITASKIRLN
ITSASRPSIFEFELFYNEDTVIDVDKDDLEKVINDANERNKDDYTVSTYNSMLEILKYAK
EIFNTDYITQPQIDEAANALNEALNNLLKRADITEAQHLLESYNDLNSELYTKASWLVFE
EARQNVNNAIQDPNELSQEQLDELCNKLTDAFVALELKNSANKYLLQIAIEMAEKASLEN
VVPAVVTEFNEALTNAKEVYAKTNATQEEVDNAFDRLANAMHMLEFYKGDKTALQKQVDD
INALDESKYIESSWQAMLPVLDKANSVLADENAMQDEVNEVYTELVKAFLNLRLKPNKDL
LQELINKANGLNAANYSAESWAVVTDVLNEAKTVLDDPEATQTQVDTIKAVLTKAIAGLQ
VEIKETSNPVKAGDTTASVATGDTITIMPIVSIGALSALIALSQINKKKKVQC

Enzyme Prediction     

No EC number prediction in MGYG000001697_01451.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	554	907	3.6e-38	0.9703264094955489
CBM32	41	166	3.2e-22	0.8387096774193549
CBM32	199	316	1e-21	0.8790322580645161

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	7.17e-59	560	908	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	2.48e-23	562	906	2	302	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	6.47e-22	429	555	2	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
COG3525	Chb	1.48e-16	431	809	136	531	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728	Glyco_hydro_20	1.45e-15	559	823	1	267	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQV05909.1	2.79e-222	13	1668	328	2019
QMW75624.1	1.27e-209	13	1643	328	1921
QPS14042.1	1.27e-209	13	1643	328	1921
QQY27139.1	9.03e-209	13	1643	328	1921
QTY17007.1	1.19e-188	328	1622	37	1598

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.11e-40	364	937	29	573	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
2RV9_A	1.45e-12	20	169	7	136	Solutionstructure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZXE_A	1.49e-12	20	169	8	137	X-raycrystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_B X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis],4ZXE_C X-ray crystal structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5. [Paenibacillus fukuinensis]
4ZY9_A	5.14e-12	20	169	8	137	X-raycrystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZY9_B X-ray crystal structure of selenomethionine-labelled V110M mutant of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
6YXZ_JJJ	1.69e-09	445	675	193	443	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	1.92e-41	364	937	51	595	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
E8MGH9	4.84e-09	1422	1635	1667	1891	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1
P26831	2.04e-07	1451	1617	1388	1566	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2
P49007	6.41e-07	510	669	279	445	Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999509	0.000490	0.000017	0.000001	0.000001	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001697_01451.