CAZyme Information: MGYG000001697_01724

Basic Information

• Species: Erysipelatoclostridium saccharogumia
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium saccharogumia
• CAZyme ID: MGYG000001697_01724
• CAZy Family: GH89
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2174	MGYG000001697_33|CGC1	245029.48	4.1566

Genome Property

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

• Gene Location: Start: 19546; End: 26070 Strand: -

Full Sequence      

MKRILKGFLVIAIIISTFVTGINNTKAVSDGEIIYPVNADAYIRSGNNANNNYNYENITQ
AHGSQYVGKNYKVINTKYYPNGSKIISVMKLELPSIEEINENKLDTYGFEFNIFKNPDFN
KSGQTYHFYYTDDVNWSETTLTWNNKPAGIGTGEILFDFTIPQGFEYESKSDDEKRIRID
ITEKIKELIEKGITAITIYVEGELKADTSLMIHSKESGDGSLGAKLVASNSNYSKNRLEQ
LINQCMSIEKKNYTKTSYDLLTASLDDAKAVLESGTTVEIDNAYAALLAAKEALIAEYPV
LEDGYIRSDKGTSVYNYENITQAHGSQYVGKDYKVINSKYYPNGNEIIGVMKFALPTLEE
ISESDFDTFKLSFNMFKNPGFNNGAQTYHFYYSDDTNWSESSLTWNNKPTSIKHDGENLL
CDFTIVQGDEYETKPDLQKAVNIDISSKIKELTKNGINEITVFVCAENKLDTSIMFHSKE
SGDGTLGAKIVGSYQNYRGQLETLINECKELDSSNYTEESFSVLTQVLNEVQQEYVEGTS
LENHVSYEKLLKAKEALVLVKDLEDIDNIAYHKPTRSNLSKTQSDKVTDGDLTTYWSGSF
YPSYVDIDLMDTYELTKLKIYTLEGKNCWYAVYGSNDGSTYDRIYQKHVDSLATNEGDEI
VFDTAQSYRILRVYIEYTQGDDKAYLTEVKAYGTALQTNEDVLKEGTLEEILDVTSYDES
EYAATITKEETIENVYGIIDRTIGEEYRNWFSFELVDDNSENDWYEISDQNDKIHIKGNE
GLSLTTGLNYYFKNYLNVHISEQTMQVNMPDELVKVNEIIKKETPYQVRYAYNYCTLSYT
FAFFGEEQWQRENDWLALNGVNVVLDLAGQEATWIKFLMNFGYSFDDAKDWLSGPAYYAW
QFMDNMESFGGPVPDGYVKDRLELARSSQRWKRSLGMQTILQGYAGMVPTNFDEYQPDVT
VIKQGNWNGFSRPDMIATDSKEYDLYAQLFYQAQEFVYGATSDYYAVDPFHEGGIRPAGL
SDATIAAEVLESMLDYDQDAVWVVQGWQSNPTNDLLKGMGDNREDHVLIVDLIKYPISDW
TKYDQTSYGSTKLDAKEFNGTSWAWGLLANFGGNPSMHGQMQVMVDDIMEAQKTSSHMVG
LGIISEAQYDNPVMYDLIFDLAWADDDFDLDDWLNRYIERRYGGTSQNAQMAWQIMKDAN
YDHGVRYTNELFGMKSKAPQDYKEQNIPYGADQLESALRLLIRDFDKFKDSECYLYDLSE
IMRQQVSNYAVLKYNDVLAAKNANDLEAFKKYKEEFLRAFEILNEVEATQQEQLGGEWIG
KAQDIAANYDDFARDSFTMNAKALITSWGSRAGHRSLKDYGWRNYEGIFKDLYTNIWSDY
LNRVEANMENGTPLNNINKNGYFDLYWKWNMADQEYTRDAKDSPEEIYEVLEKVLENCAI
SGDVDANIGNLALTGIVKDSNDLKADVNAVNDGDATTIYSFKAKDEKAPQVIVDLIGVFQ
LSEIDVIVNDTYDYEIWVSEDNVDWLKIGDGISDETKFAVQGSVRYIKLVGINNIAQLSI
GEIRAYGERVLPTLNQLENLIEFCESINTSGNEESKITDFNNILNSAKKAVDNEAAPDEI
NTVYWNLYDAVTDLNLSGIFNLSLNKPVTAHNDPSGKSANLVDGNLSSAWDAGRLSLTGA
PYEDKITPAWAIVDLKEEYQISEIEINFGSNVWHHYTVYGSVDGEEWFEIGNKDTDSLPN
DIEDTYKLENTFARYIKLEITNVQLESSGKRTPVKVNELIIIGKMKDLLDKEALQQQVAF
AKAIDLEKYQDGIEKDTFIIILTKAIEILDSATTQQEIDNVLTALNEAIEALESINIEDK
TALQIAVDTANTLKTQGALDNVVPAVVNEFEAALAEAEGILADNYADQITIDTSFYRLAN
AIHMLDFVKGDKSALEALLEEANGHEEENYTTDSWTALQEAIEAATEVMNDENALESDVT
EALNNLTNAIGNLVLRADKTRLQEAYDMVNGLDKSLYTEASVAGITEPMTNAKAVLDDPD
ATQAEVDSAYEALIRAYLDMRLIPNKDLLQDLINKANGLNAANYSAKTWNVMQDALEKAK
ATLTDANATQEEVDNAKEVLTKAMAGLETSNSVKAGDTTASVATGDSASIIQILSMLVML
GTLVIMVNVKKIED

Enzyme Prediction     

No EC number prediction in MGYG000001697_01724.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH89	771	1427	3e-182	0.9864253393665159
CBM32	1650	1778	1.5e-20	0.8870967741935484

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05089	NAGLU	2.16e-114	829	1161	1	329	Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold.
pfam12972	NAGLU_C	6.78e-37	1175	1427	3	256	Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold.
pfam12971	NAGLU_N	2.15e-23	735	813	3	80	Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold.
pfam00754	F5_F8_type_C	6.83e-11	1653	1761	9	113	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
NF033679	DNRLRE_dom	1.06e-08	64	227	7	162	DNRLRE domain. The DNRLRE domain, with a length of about 160 amino acids, appears typically in large, repetitive surface proteins of bacteria and archaea, sometimes repeated several times. It occurs, notably, three times in the C-terminal region of the enzyme disaggregatase from the archaeal species Methanosarcina mazei, each time with the motif DNRLRE, for which the domain is named. Archaeal proteins within this family are described particularly well by the currently more narrowly defined Pfam model, PF06848. Note that the catalytic region of disaggregatase, in the N-terminal portion of the protein, is modeled by a different HMM, PF08480.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMN35090.1	1.68e-163	576	1708	47	1135
AOY53263.1	3.05e-161	576	1708	47	1135
AXH51964.1	4.13e-161	576	1708	47	1135
ALG48242.1	7.56e-161	576	1708	47	1135
BAB80572.1	1.38e-160	576	1708	47	1135

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VC9_A	8.96e-169	576	1441	13	880	Family89 Glycoside Hydrolase from Clostridium perfringens in complex with 2-acetamido-1,2-dideoxynojirmycin [Clostridium perfringens],2VCA_A Family 89 glycoside hydrolase from Clostridium perfringens in complex with beta-N-acetyl-D-glucosamine [Clostridium perfringens],2VCB_A Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with PUGNAc [Clostridium perfringens],2VCC_A Family 89 Glycoside Hydrolase from Clostridium perfringens [Clostridium perfringens]
7MFK_A	1.13e-168	576	1441	21	888	ChainA, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
4A4A_A	1.19e-167	576	1441	36	903	CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
4XWH_A	5.32e-67	773	1416	51	692	Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54802	4.43e-66	773	1416	74	715	Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2
Q9FNA3	5.28e-66	773	1384	94	751	Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
E8MGH9	6.76e-11	1931	2108	1667	1856	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	1.06e-06	1893	2053	1389	1561	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH 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
0.000563	0.967256	0.031477	0.000249	0.000227	0.000192

TMHMM  Annotations     

start	end
2150	2169