CAZyme Information: MGYG000002310_02253

Basic Information

• Species: Microvirga massiliensis
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Microvirga; Microvirga massiliensis
• CAZyme ID: MGYG000002310_02253
• CAZy Family: GH109
• CAZyme Description: Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
336		36091.2	4.8099

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002310	8892798	Isolate	not provided	not provided

• Gene Location: Start: 377425; End: 378435 Strand: -

Full Sequence      

MEKLPATSLARPRLGFLGVGWIGRLRMEAILAADAVEVAAIAEPSPDMAAAARQLAPDAA
MVSTLDDLLDLGVDGVVIATPSALHAEQSIRALERGAAVFCQKPLGRTEAEVRTVVEAAR
AADRLLGVDLSYRFTEGMRRIRDLVRSRELGRIYAVDLIFHNAYGPDKAWFYDPVLSGGG
CVMDLGVHLVDLALWTLDCPGVSAVSGKLFADGEQLGPRPDRVEDYAVATLELDTGAVVQ
LACSWRLQAGCDAMISAAFYGTGGGAALRNVDGSFYDFRAERYRGTAREVLANPPDAWGG
RAGVDWAMRLAAGERFDPAAERLVDVARVLDRIYGR

Enzyme Prediction     

No EC number prediction in MGYG000002310_02253.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH109	12	154	4.1e-17	0.38095238095238093

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0673	MviM	2.44e-48	13	335	5	330	Predicted dehydrogenase [General function prediction only].
pfam01408	GFO_IDH_MocA	4.91e-13	13	129	2	119	Oxidoreductase family, NAD-binding Rossmann fold. This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
pfam02894	GFO_IDH_MocA_C	3.40e-07	142	315	1	159	Oxidoreductase family, C-terminal alpha/beta domain. This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
PRK10206	PRK10206	0.002	78	191	70	180	putative oxidoreductase; Provisional
PRK11579	PRK11579	0.002	78	231	70	216	putative oxidoreductase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VTU39411.1	2.04e-145	1	336	2	343
QRA09938.1	1.83e-15	8	252	6	251
QPS45215.1	8.46e-15	13	268	11	265
BCS38310.1	2.55e-14	7	204	25	229
QQM91678.1	3.90e-14	7	252	5	252

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JW6_A	1.02e-30	13	264	6	267	Thecrystal structure of KanD2 in complex with NAD [Streptomyces kanamyceticus],6JW6_B The crystal structure of KanD2 in complex with NAD [Streptomyces kanamyceticus],6JW7_A The crystal structure of KanD2 in complex with NADH and 3'-deamino-3'-hydroxykanamycin A [Streptomyces kanamyceticus],6JW7_B The crystal structure of KanD2 in complex with NADH and 3'-deamino-3'-hydroxykanamycin A [Streptomyces kanamyceticus],6JW8_A The crystal structure of KanD2 in complex with NADH and 3'-deamino-3'-hydroxykanamycin B [Streptomyces kanamyceticus],6JW8_B The crystal structure of KanD2 in complex with NADH and 3'-deamino-3'-hydroxykanamycin B [Streptomyces kanamyceticus]
6NOR_A	6.42e-20	4	250	15	258	Crystalstructure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora],6NOR_B Crystal structure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora],6NOR_C Crystal structure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora],6NOR_D Crystal structure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora],6NOR_E Crystal structure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora],6NOR_F Crystal structure of GenD2 from gentamicin A biosynthesis in complex with NAD [Micromonospora echinospora]
2GLX_A	1.20e-19	13	240	2	226	ChainA, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens],2GLX_B Chain B, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens],2GLX_C Chain C, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens],2GLX_D Chain D, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens],2GLX_E Chain E, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens],2GLX_F Chain F, 1,5-anhydro-D-fructose reductase [Ensifer adhaerens]
3E18_A	5.53e-19	8	241	2	226	CRYSTALSTRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua],3E18_B CRYSTAL STRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua]
1EVJ_A	2.25e-14	70	245	67	242	ChainA, GLUCOSE-FRUCTOSE OXIDOREDUCTASE [Zymomonas mobilis],1EVJ_B Chain B, GLUCOSE-FRUCTOSE OXIDOREDUCTASE [Zymomonas mobilis],1EVJ_C Chain C, GLUCOSE-FRUCTOSE OXIDOREDUCTASE [Zymomonas mobilis],1EVJ_D Chain D, GLUCOSE-FRUCTOSE OXIDOREDUCTASE [Zymomonas mobilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P77503	3.92e-21	52	268	48	278	D-glucoside 3-dehydrogenase OS=Escherichia coli (strain K12) OX=83333 GN=ycjS PE=1 SV=1
P49307	2.12e-19	9	195	1	182	Rhizopine catabolism protein MocA OS=Rhizobium meliloti OX=382 GN=mocA PE=3 SV=1
Q2I8V6	3.16e-18	13	240	3	227	1,5-anhydro-D-fructose reductase OS=Ensifer adhaerens OX=106592 GN=afr PE=1 SV=1
A5G0Y2	1.15e-15	13	236	4	219	Inositol 2-dehydrogenase OS=Acidiphilium cryptum (strain JF-5) OX=349163 GN=iolG PE=3 SV=1
Q7BUE1	1.15e-14	13	245	4	247	Putative UDP-kanosamine synthase oxidoreductase subunit OS=Amycolatopsis mediterranei (strain S699) OX=713604 GN=rifL PE=1 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
1.000061	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002310_02253.