CAZyme Information: MGYG000000817_00785

Basic Information

• Species: Catenibacterium sp900540665
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Catenibacterium; Catenibacterium sp900540665
• CAZyme ID: MGYG000000817_00785
• CAZy Family: GH84
• CAZyme Description: Hyaluronoglucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1741	MGYG000000817_18|CGC1	195447.35	4.8662

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000817	2136964	MAG	China	Asia

• Gene Location: Start: 21149; End: 26374 Strand: +

Full Sequence      

MKGKKVITYAVSFLVALGCVSAFPMTVQADTGYEVYPNPHTMSYSDGDYEMTSQVNVVYE
DGIDADTKARLNEVLALKGMNASVSSEKKAGKTNILVGVKGSKQYVDSQFGTTSEGLFDK
LDSYALKSDKGTISILGKDTDAAFYGLTSLYHIFKQVEGKTIRNFSIEDYADVASRGFIE
GYYGNPWSTEDRCKLMEWGGYYKLNSYFYAPKDDPKHNGKWRELYTDQEIETKIKPLAEA
GNKSKCRFVFALHPYMNNPIRYNSEANYQADLKVMQAKFKQVIDAGVRQIAILADDAPNV
GGANYTRTLTDMSNWLKELQPSYPGLKLTLPFCTQEYMGWGQSYYRDFPENVQIIMTGGR
VWGEVTNNFTSSFTNTAGRGPYMWINWPCTDNSKKHLIMGGYTTFLHPGVDPSKIQGIVL
NPMQQSEPSKVAIFGNACYSWNIWQTEEEANKCYNDSFKYVDHNGYEETEASTALRELSK
HMINQNMDSRVTRLEESVELRDKLQAFKTKLTKGEKISDEEFDEMINAFTVLQNASKIYR
ESGNERIKSQIVYWLNCWDDTTNAALNYIKGIQAAQNEEANATIWDYFSAAQAAFEKSKS
YGFHYVDHLEYAEVGVQHIVPFIKSLDSYLSEIASTIVNPDKQIAKYITNREDTPAGKED
NIFDGNASTELVYKSPNSIFTGTYVGIKYSKAIDVNHVIFRVGANSNPRDTFLKAKVQYT
TDGKNWTDVNDTEYDLPNNVELTDLNLKGVKGIRMIATADKSNTWLGVRDILVNPTTTPS
SPADKGTLSLTKLTLKGGSLDNLLDDNESSYAHFAESPYKGGEIKDYIPVDAAVTLTFNN
PKKLGTINFSQDGGTDKLTKYVLEYTADGETWKTLKEYAGDATVHLNVEDQDITAKAIRV
RNLELHLSSNTAGYWWKLKTFNHTDVVNEYDDKAVYTNTDYKLHSKSTLDRTDLVYKKEM
TLAPKQYVGVKLSRVKDLKQLELDYTGDVVVEASVNAHDWVEVTDLNNNLPDARYVRLIN
KKSSDVKLTLNKFVVHSTEVTAPYLYKTTMTINPSWGVAEDTRNNGAAFDGNIDSTTEFG
DLPQKGQYIIYDLGQMRNIDKLAMYCQDSAVNYIRDATISVSSDLENWTDVVTIGDGVEN
IGDAGVQCIDSDAGYKASSTYPNKVYVSGTANHVPARYLRILFTASNNNRAVVFNEIMIN
DGEYAPEDNDPTFESSVTEAKGYKPQYMIDGDLLTSYKPGSNKAGYLTYTLSDRLNVKKF
NIIQKGEISNAKVYALIDKEVTTRNVPEENREWVQLGTLRKSLNEFYIPHGNVYKLKFEW
EENHIPTISEIITLTDEEYKSECAKDLKNYIDSLHVEEDKYTATSYNAYKTARDAALNAY
NTQMGEKDALEEAKANLKTAHEGLTALGDLKALEAEIKALDKLSKDDYTEESYQALMAVK
AEAEILLKNEDASVEEVDAMLEQLATAKAALVTKVSISKKTLRDYIDSNNLNTLDTSIYL
TSTVTPFKDALNNAEDILNKENATVTEVEDAYKALHEARKNLVLKATDAEVKALENKMAS
YKEEDYTASSWKEFVLVLDEIREELKAEHTSEEITALTEKLDTASKKLVRRGNTAELDLL
LAQAKKTDSKLYTEKSYKNLLEVIKAVEKALENKAELTQEEVDALTKDLRDAMEVLEKLP
VITPSKPEEKPTTPSKPEETTKPEVKPSTKPATGDTTMVGLFAFFSMISLLGYVLLKKKE
A

Enzyme Prediction     

EC	3.2.1.35	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH84	176	479	2.4e-98	0.9932203389830508

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07555	NAGidase	4.14e-115	176	478	1	293	beta-N-acetylglucosaminidase. This family has previously been described as a hyaluronidase. However, more recently it has been shown that this family has beta-N-acetylglucosaminidase activity.
pfam02838	Glyco_hydro_20b	5.92e-24	33	169	2	123	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
TIGR02169	SMC_prok_A	3.28e-08	1390	1679	172	467	chromosome segregation protein SMC, primarily archaeal type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
COG1196	Smc	1.57e-07	1440	1678	174	390	Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning].
pfam00754	F5_F8_type_C	3.91e-07	1067	1193	16	122	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCL58377.1	0.0	2	1739	4	1871
QMW73896.1	0.0	5	1740	24	1891
QPS12837.1	0.0	5	1740	24	1891
QQY28346.1	0.0	5	1740	24	1891
QQV04685.1	0.0	5	1740	24	1891

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6PV4_A	3.49e-226	33	639	32	653	Structureof CpGH84A [Clostridium perfringens ATCC 13124],6PV4_B Structure of CpGH84A [Clostridium perfringens ATCC 13124],6PV4_C Structure of CpGH84A [Clostridium perfringens ATCC 13124],6PV4_D Structure of CpGH84A [Clostridium perfringens ATCC 13124]
6PWI_A	6.07e-109	33	632	34	626	Structureof CpGH84D [Clostridium perfringens ATCC 13124],6PWI_B Structure of CpGH84D [Clostridium perfringens ATCC 13124]
2CBI_A	2.95e-49	37	443	18	421	Structureof the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase [Clostridium perfringens],2CBI_B Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase [Clostridium perfringens],2CBJ_A Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase in complex with PUGNAc [Clostridium perfringens],2CBJ_B Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue of human O-GlcNAcase in complex with PUGNAc [Clostridium perfringens],2V5C_A Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure [Clostridium perfringens],2V5C_B Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure [Clostridium perfringens],2VUR_A Chemical dissection of the link between Streptozotocin, O-GlcNAc and pancreatic cell death [Clostridium perfringens],2VUR_B Chemical dissection of the link between Streptozotocin, O-GlcNAc and pancreatic cell death [Clostridium perfringens],2X0Y_A Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds [Clostridium perfringens],2X0Y_B Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds [Clostridium perfringens]
5OXD_A	3.71e-49	37	443	20	423	Complexof a C. perfringens O-GlcNAcase with a fragment hit [Clostridium perfringens]
2J62_A	3.97e-49	37	443	18	421	Structureof a bacterial O-glcnacase in complex with glcnacstatin [Clostridium perfringens],2J62_B Structure of a bacterial O-glcnacase in complex with glcnacstatin [Clostridium perfringens],2WB5_A GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation [Clostridium perfringens],2WB5_B GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26831	0.0	4	1538	6	1564	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2
Q8XL08	3.35e-48	4	443	7	451	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53	3.13e-47	4	443	7	451	O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
Q89ZI2	9.60e-41	52	573	39	538	O-GlcNAcase BT_4395 OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_4395 PE=1 SV=1
O60502	1.31e-19	177	433	63	325	Protein O-GlcNAcase OS=Homo sapiens OX=9606 GN=OGA PE=1 SV=2

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
0.000576	0.807837	0.190729	0.000299	0.000283	0.000239

TMHMM  Annotations     

start	end
7	29
1717	1736