CAZyme Information: MGYG000001423_02070

Basic Information

• Species: Clostridium celatum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium celatum
• CAZyme ID: MGYG000001423_02070
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1333	MGYG000001423_55|CGC1	151864.48	4.217

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001423	3553421	Isolate	not provided	not provided

• Gene Location: Start: 7623; End: 11624 Strand: +

Full Sequence      

MRKKGELKIYCKIFVIIFLFNMLISPITNIFANEVKAEVKDTYGINLALNKEVEVSGTET
SSLTGDKAVDGDYTDDNSRWSSATVTDSNPQWLYVDLEKEYIIEEINIRWQNWAYGTEFK
VQKSNNGEEWTDIALLTNPLGKDEANKNLVNIVDVEQESARYIRVYITKRNQWTSVSIRE
LEVIGYEIKEGNIAEGKKATVSAVENNSTVWTADKVIDGDKESDDSRWASPTMPVIPTET
DTHWVSIDFGKIVEMDSVNIHWYKKAWAENAIIQISNDGENFEDIETIIHEAGDTLNLVD
TVQFAEVKTGRYLRVFIAERNANAYNNVSIREIEVIGREKYIPELDMTCEQVINSITTLG
EITIDTTELTLPEVPRGFGIRVRGSEFENIVTNDGVITRHNINDANVSILLEVYKESDDT
KTATKNIVVTIPGKSSLYPEIFPEVSEQNDVPKVIPSLQEWYGLNGSFTLTENSRILIND
VNNVDLNKVADLFNDDLKYFTDIELEVVEVSSEEEVKPGDIYIESIDENGYDLGKEGYFT
IIDNSIKIYSPTYTGNLYGTVTLLQILWQAEDELNIPCGIIRDYPKYEIRGVMLDVARMP
MRIEFVRDYAKILSWYKLNEFHLHLNDNQWSDGDYKNPEAWNDVYNAFRLESKEHPGLKP
SNSDLNDPYYTQEEFIELELMAMDYGMEVVPEIDSPAHSLPFTKYMRELGTPIHNTKYWF
DHIDIENEDGKNLIKGLLDEFIDGTDENEPVFLGNTVHLGIDEYDTSVGDKFRQYTSEMS
NYVLEKGKTPRVWGSLKQFSGTTMLPEGTVIDVWSMAWEDVNARIKEGYEIVNVPQPFTY
ITPSRWHKDFMNTQNVYNNWEPNDFNGVKLPLGEPQLLGGKMAIWGDESMEGIVEADLHE
RLLPAVATVGEKTWSGTREDKDYLEFMKTFNALEEGPNTTIQNEIVSENELVVKYNFEDE
TASDSSLNKYDASIVNGEVVQVENNKVLTLKGNTTLETPLQSLTYPYTATFDVKVDELGK
TINLFAGYDGELKIKEDGTLSIRRSFYEQDFDFKVKEEEWNEITLVGTFQALALYVNGEF
VQQLHSYRDHSNNIISGQELHATFVLPLEKIGENLKGQMDNIEVYNTAMPEEWIAGDKNA
KLNLACGADAYSSSNSLLYTKEWRAVDGDSRNGDSKWISQNSDNQWLLIDLKEVKQISEV
KLLFAEAATEYKILTSIDGVNFEEVSHITSNTKTEVVSEFDLKNIRYIKFQGVKRGGNNG
YSILELQAFGENVQEEKSADFNNDGVIDLKDLAIASRYYGQNNKEYDLDGDGKVGIYELQ
KISDIILSDNRRI

Enzyme Prediction     

No EC number prediction in MGYG000001423_02070.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	583	916	6.2e-62	0.9703264094955489
CBM32	56	181	3.4e-21	0.9032258064516129
CBM32	1151	1267	4.6e-19	0.9274193548387096
CBM32	202	334	4.4e-18	0.9516129032258065

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	4.61e-109	588	916	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	4.24e-48	589	915	1	303	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.
pfam00728	Glyco_hydro_20	6.04e-38	587	916	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	3.91e-35	587	928	1	355	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. 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.
cd06568	GH20_SpHex_like	9.21e-31	587	926	1	325	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXH51903.1	0.0	2	1327	4	1327
AMN35076.1	0.0	1	1327	1	1327
ASY50997.1	0.0	2	1327	4	1327
AWS25495.1	0.0	2	1327	4	1327
QQA11576.1	0.0	2	1327	4	1327

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	1.32e-74	368	1124	18	731	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A	7.59e-30	452	918	34	478	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]
3GH4_A	4.96e-25	436	926	26	501	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
6YXZ_JJJ	5.85e-23	536	928	259	695	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
7BWG_A	6.75e-23	536	932	87	493	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	2.17e-77	343	1124	16	753	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
Q9SYK0	1.45e-20	555	921	138	529	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
P06865	1.78e-18	540	915	119	486	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2
Q5RC84	2.36e-18	540	915	119	486	Beta-hexosaminidase subunit alpha OS=Pongo abelii OX=9601 GN=HEXA PE=3 SV=1
Q8WSF3	3.75e-18	516	922	204	618	Probable beta-hexosaminidase fdl OS=Drosophila melanogaster OX=7227 GN=fdl 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
0.003878	0.995154	0.000370	0.000190	0.000181	0.000182

TMHMM  Annotations     

start	end
13	32