CAZyme Information: MGYG000001262_01614

Basic Information

• Species: Sphingomonas ginsenosidimutans
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingomonas; Sphingomonas ginsenosidimutans
• CAZyme ID: MGYG000001262_01614
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1607	MGYG000001262_55|CGC1	167325.49	4.6127

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001262	3667136	MAG	Italy	Europe

• Gene Location: Start: 5623; End: 10446 Strand: +

Full Sequence      

MAITHNLSIKVSGTEASGKPAFSVFVNGVAVATNVEVGADYRLGQWNTFTFSYQSDSAND
DIRIVYANDHHDSATGQDRNLYINELALDGRTFQAALATGANAHLGYQAGLTSAALFSNG
SLSFSTSQFMTSTPGALQYLGIAYSGAEFTTNQLADWHLPVVFPTDANLDYYASKGMNIL
RLPILWEQLQPTKGGAFDQAYIDRITHVIDYAATKGMTIVVDVHNFGRAYGELIGGPVVT
NADFAAMWGALGGALKDRGNVMLGLMNEPNEQTPADWLASANAAIAAIRAAGAAQTILVA
GSAWDGAYNWLTSGNAATIGKGVVDPLDKYAFEVHQYLDLTASGGVATPVSADIGVQRLQ
AITQWALQNNQKLFLGEFGVGTDATSLSALDKMLTYMAQHADAWLGGTYWAAGNNNYFSI
DPVGGSDRPQMNLLEKYAPAPITAIENATAVTYTSGNTTYYADGSVEVRSFQSDGTLRGK
TITHVNGSKETYALNIVGQAYTTEYSTFDAKGALISLTRTQADGKMVFGKTVNNALGRTT
SDQYNTAGLLTTRTIEQPGVVETKNYAADGFTLLRHIVQQTGGLKDVWIYGITGQTYTQA
HEQYAANGTLTSLTRMRADNSLVFTKTVDLATGAVATGSYSNAGVLTSMLIVQGAETTQK
TYAADGATVTRSILNHADGSKEVWYYGQTDPNYRTVHETYNAAGAMVSVERLRGDGSLYY
SRDVLSDGKVVTVTNSFTTDGLLTTSVIGRSDGSITTKTFASDGIALLQDVTTTADGARE
VHLYGVTGAAYTATGGAKADVLVGGAGNDTLTGGGGNDTLTGGAGVDTFVFARGSGNDTI
TDFGRNGEADKLDLSAYLTAGLRPTVAASGSDTLLTFTTGETIRLTAVDPARLTATATGY
TFTAPVASRPITLPGVVDSALGTVGGVVGGIVTTPVSVALDLRAQNAGQAWSFTSAAGVN
RFEVRAGDHWSGDGTAGKERSETYATAKLDLGKTYHLTFDVMVEAGAKNTASWMTLMQLQ
STFDPGDAPHSPPFALEMVGDKMRIVTRSSATSIMAVDDSVYQRHFTDTADITRGKWYAF
DVTVKFLPGGDGRLTVVRDGVTIVDYTGPLGFQDAVGPYLKQGVYRADAPETIAVNYRNT
ALELVPNSTAPAPSAPSNLTLSVADVAENGAPGALVGTAAATDAQGRAISYSLVDSAGGM
FAIDPQTGKIVTAKTLDYETQKAHSITVRATGSNGLFVDKAVTVGVTDVNEAPVSVTLAG
GKVAENLAAGAIVGTVSAIDPEARTLTYSLVGGTGMPFSIDARTGVITTTAPLDYETRSS
YALSVRATDVGGLSTDKAVTIGVTDVNEAPANLTLTGGTVTENMAAGTIVGTARAADPDG
NTLSYSLVGASGLPFAIDARTGVITTTAPLDYEARNAYSLTVRASDPGGLKVDKLVSIGV
TDVNEAPVDLALAGGKVAENLAPGALAGVARASDPEGLALSYSLVNAKGMPFAIDARTGV
ITTTAALDYEGKGSYALTIRATDAGGLTVDKAVTIGVIDMPELPKGWVSFNASREPAPDR
SGLTDAHSLGGGTGMVADAHGDYTFVVPDHPDGLIKLGADYFDPHVI

Enzyme Prediction     

EC	3.2.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	139	414	8.1e-93	0.975177304964539

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	4.01e-40	163	416	24	272	Cellulase (glycosyl hydrolase family 5).
cd11304	Cadherin_repeat	5.48e-24	1263	1348	6	97	Cadherin tandem repeat domain. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.
pfam14099	Polysacc_lyase	4.61e-23	961	1128	35	197	Polysaccharide lyase. This family includes heparin lyase I, EC:4.2.2.7. Heparin lyase I depolymerizes heparin by cleaving the glycosidic linkage next to an iduronic acid moiety. The structure of heparin lyase I consists of a beta-jelly roll domain with a long, deep substrate-binding groove and an unusual thumb domain containing many basic residues extending from the main body of the enzyme. This family also includes glucuronan lyase, EC:4.2.2.14. The structure glucuronan lyase is a beta-jelly roll.
cd11304	Cadherin_repeat	1.21e-22	1359	1445	5	97	Cadherin tandem repeat domain. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.
cd11304	Cadherin_repeat	2.64e-19	1166	1251	6	97	Cadherin tandem repeat domain. Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARN23933.1	4.92e-71	134	437	35	345
AEL04963.1	7.14e-71	136	438	22	334
ATU68615.1	2.04e-70	134	437	83	393
QOF07261.1	2.45e-70	136	438	22	334
QXJ19104.1	2.45e-70	136	438	22	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HOS_A	1.61e-62	137	438	27	337	Crystalstructure of the endo-beta-1,4-glucanase Xac0029 from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
5HNN_A	8.80e-62	137	438	22	332	Crystalstructure of the endo-beta-1,4-glucanase (Xac0030) from Xanthomonas axonopodis pv. citri with the triple mutation His174Trp, Tyr211Ala and Lys227Arg. [Xanthomonas citri pv. citri str. 306],5HNN_B Crystal structure of the endo-beta-1,4-glucanase (Xac0030) from Xanthomonas axonopodis pv. citri with the triple mutation His174Trp, Tyr211Ala and Lys227Arg. [Xanthomonas citri pv. citri str. 306],5HNN_C Crystal structure of the endo-beta-1,4-glucanase (Xac0030) from Xanthomonas axonopodis pv. citri with the triple mutation His174Trp, Tyr211Ala and Lys227Arg. [Xanthomonas citri pv. citri str. 306]
5HPC_A	7.56e-61	137	438	22	332	Structureof XacCel5A crystallized in the space group P41212 [Xanthomonas citri pv. citri str. 306]
4W7U_A	1.21e-60	137	438	22	332	Crystalstructure of XacCel5A in the native form [Xanthomonas citri pv. citri str. 306],4W7V_A Crystal structure of XacCel5A in complex with cellobiose [Xanthomonas citri pv. citri str. 306],4W7W_A High-resolution structure of XacCel5A in complex with cellopentaose [Xanthomonas citri pv. citri str. 306]
5I77_A	3.83e-49	138	437	3	301	Crystalstructure of a beta-1,4-endoglucanase from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P17974	8.20e-66	135	437	115	424	Endoglucanase OS=Ralstonia solanacearum OX=305 GN=egl PE=1 SV=2
P58599	1.22e-64	135	437	113	422	Endoglucanase OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=egl PE=3 SV=1
O74706	2.18e-49	138	437	33	330	Endo-beta-1,4-glucanase B OS=Aspergillus niger OX=5061 GN=eglB PE=1 SV=1
A2QPC3	2.18e-49	138	437	33	330	Probable endo-beta-1,4-glucanase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=eglB PE=3 SV=1
Q96WQ8	6.52e-48	138	437	33	331	Probable endo-beta-1,4-glucanase B OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=eglB 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
1.000058	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001262_01614.