CAZyme Information: MGYG000000272_01190

Basic Information

• Species: Prevotella hominis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella hominis
• CAZyme ID: MGYG000000272_01190
• CAZy Family: GH51
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
874	MGYG000000272_12|CGC1	98418.4	6.0473

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000272	3991064	Isolate	China	Asia

• Gene Location: Start: 11302; End: 13926 Strand: +

Full Sequence      

MKMNHKILLASTAILSFTSLMASGKLNPKGNPAFWDEQNAPAYSVMGKDTTCQVFLYSPD
PTQGLHLAYLSDNEKWIEVGQLCASDYGPWGSGKKMYSPSVVQANDGTWRALWSVGELFP
QFAVAYSEDLVTWRPQDYPIVAEKGVKSPVAYQMEDGNFDIYIKTAKGKRYVQASQDFRT
FVEDSLEASADEILWDKDSVLINGKMQKGDEFEIPAVHLNYIRAWFKALDEENRENNRQI
PKTNQELAALVKEYNDRQVAMHGEKAVLTQMDESDRIEAKLVVDGKQTKRISDKLIGIFF
EDISRAADGGLCAELLQNGDFEYNKDDRKHSWNATTAWQGVDLSSVSVENGVSKNNPHYA
VLGATPIYNIGWDGISILRGARDAKKEGKHAASYYDVSLYARCLNGKNKQLMVALVDEAG
DVISQAKVKVVGNEWSEYKAQLVITDKYQGNLEEGKGIRFALIPKGETQVGIDLVSLKPH
DTYKGHGLRKDLAEKIAELKPKFVRFPGGCMLHGQGLDNIYHWKETVGPLKDRKPARNLW
NYHQTRQLGFYEYFQWCEDMGAEPLPVLAAGVPCQNSQPNAQGLCGQQGGIPMDQMPQYV
QDVLDLVEWANGDPATSSWAKMRADAGHPAPFNLKMIGIGNEDLISTTFKERYLMICKAL
KQKYPDIEVVGTVGPFHYPSSDYVEGWKIAKENRQYIDAVDEHYYEKPGWFINHQDYYDH
YDRSMPKVYLGEYAANGNNEVDRALAEGIHLCNVERNGDVVEMASYAPLLCKDGYANWNP
DMMYFNNNKVRATESYQVQKMFSVHSGDVYIASDLQLPEVLKRYVGVSVVKDSKSGKVWL
KIVNSLPRTLKLKLSGLTQKEIEIGPRQSNVWAL

Enzyme Prediction     

No EC number prediction in MGYG000000272_01190.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	471	862	3.1e-95	0.5952380952380952

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3534	AbfA	7.37e-35	444	855	17	437	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964	Alpha-L-AF_C	4.33e-25	731	858	1	143	Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
smart00813	Alpha-L-AF_C	2.31e-24	744	863	23	145	Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
pfam02018	CBM_4_9	2.47e-06	313	450	1	123	Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT66325.1	0.0	37	874	33	866
VEH15278.1	0.0	3	857	1	804
BCS84266.1	0.0	41	857	44	824
AGB28163.1	0.0	37	858	20	802
QVJ81530.1	8.33e-300	50	858	34	801

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZPS_AAA	8.29e-63	281	845	3	555	ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]
3S2C_A	2.07e-15	487	730	48	252	Structureof the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
4ATW_A	3.61e-15	487	730	48	252	Thecrystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8]
3UG3_A	3.94e-15	487	730	68	272	Crystalstructure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima]
2VRQ_A	3.59e-10	486	844	50	420	StructureOf An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_B Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_C Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P82593	6.40e-115	291	813	48	547	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
Q9SG80	5.85e-75	265	816	29	553	Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1
Q8VZR2	2.34e-71	281	855	42	590	Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1
Q0CTV2	1.30e-56	275	808	24	529	Probable alpha-L-arabinofuranosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfA PE=3 SV=1
Q2U790	1.80e-56	281	844	28	561	Probable alpha-L-arabinofuranosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abfA PE=3 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
0.000727	0.998304	0.000319	0.000243	0.000207	0.000181

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000272_01190.