CAZyme Information: MGYG000002310_00986

Basic Information

• Species: Microvirga massiliensis
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Microvirga; Microvirga massiliensis
• CAZyme ID: MGYG000002310_00986
• CAZy Family: GH0
• CAZyme Description: CDP-paratose 2-epimerase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
370		40894.36	7.7984

Genome Property

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

• Gene Location: Start: 1013935; End: 1015047 Strand: +

Full Sequence      

MTDATSPVKPTVLRRRPILITGGAGFIGSNLADRLASEGRDVLVLDALSREGVERNLAWL
KSRHPERISSVIADIRDEAAVANAAAEAQAVFHLAAQVAVTTSLDNPREDFDINLRGTIH
LLEALRRRNERTPLLFASTNKVYGDLADVVLERTGDAYLPADVSLRGTGIGEDRPLDFHT
PYGCSKGAADQYVLDYARSFGVPTCVLRMSCIYGQRQMGTEDQGWVAHFLIRALKGEPIV
IYGDGCQVRDVLDVQDAIEAYVNAWMRIDRVAGHAFNLGGGTANAISLRQLLAYMESLLG
QRVATNFSDWRAGDQRYYVSDTRRAHQQLGLRTPRPWKDGIAALLAWLREENAPVRRQRA
APLHRAEARP

Enzyme Prediction     

No EC number prediction in MGYG000002310_00986.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05258	CDP_TE_SDR_e	3.54e-129	16	348	1	337	CDP-tyvelose 2-epimerase, extended (e) SDRs. CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
cd05256	UDP_AE_SDR_e	1.67e-63	18	347	2	303	UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
COG0451	WcaG	4.76e-58	18	351	3	311	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
cd08946	SDR_e	1.19e-51	18	279	1	200	extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
pfam01370	Epimerase	5.42e-48	18	279	1	238	NAD dependent epimerase/dehydratase family. This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKE91467.1	3.42e-152	9	351	350	697
QSW94569.1	1.06e-136	3	362	315	679
AXV15253.1	3.00e-136	17	350	330	663
QTV00804.1	5.99e-136	17	348	330	661
ANK87832.1	8.23e-136	17	348	329	660

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ORR_A	5.68e-82	18	347	4	335	ChainA, CDP-tyvelose-2-epimerase [Salmonella enterica subsp. enterica serovar Typhi],1ORR_B Chain B, CDP-tyvelose-2-epimerase [Salmonella enterica subsp. enterica serovar Typhi],1ORR_C Chain C, CDP-tyvelose-2-epimerase [Salmonella enterica subsp. enterica serovar Typhi],1ORR_D Chain D, CDP-tyvelose-2-epimerase [Salmonella enterica subsp. enterica serovar Typhi]
6WJB_A	9.16e-38	18	344	6	306	UDP-GlcNAcC4-epimerase from Pseudomonas protegens in complex with NAD and UDP-GlcNAc [Pseudomonas protegens Pf-5],6WJB_B UDP-GlcNAc C4-epimerase from Pseudomonas protegens in complex with NAD and UDP-GlcNAc [Pseudomonas protegens Pf-5]
6WJ9_A	4.85e-37	18	344	6	306	UDP-GlcNAcC4-epimerase mutant S121A/Y146F from Pseudomonas protegens in complex with UDP-GlcNAc [Pseudomonas protegens Pf-5],6WJ9_B UDP-GlcNAc C4-epimerase mutant S121A/Y146F from Pseudomonas protegens in complex with UDP-GlcNAc [Pseudomonas protegens Pf-5],6WJA_A UDP-GlcNAc C4-epimerase mutant S121A/Y146F from Pseudomonas protegens in complex with UDP-GalNAc [Pseudomonas protegens Pf-5],6WJA_B UDP-GlcNAc C4-epimerase mutant S121A/Y146F from Pseudomonas protegens in complex with UDP-GalNAc [Pseudomonas protegens Pf-5]
4ZRM_A	3.83e-35	18	350	6	309	CrystalStructure of UDP-Glucose 4-Epimerase (TM0509) from Hyperthermophilic Eubacterium Thermotoga maritima [Thermotoga maritima MSB8],4ZRM_B Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) from Hyperthermophilic Eubacterium Thermotoga maritima [Thermotoga maritima MSB8],4ZRN_A Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) with UDP-glucose from Hyperthermophilic Eubacterium Thermotoga Maritima [Thermotoga maritima MSB8],4ZRN_B Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) with UDP-glucose from Hyperthermophilic Eubacterium Thermotoga Maritima [Thermotoga maritima MSB8]
6LTT_A	8.98e-32	19	352	4	312	ChainA, UDP-glucose 4-epimerase [Mycobacterium tuberculosis H37Rv],6LTT_B Chain B, UDP-glucose 4-epimerase [Mycobacterium tuberculosis H37Rv]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14169	2.36e-81	18	347	3	334	CDP-paratose 2-epimerase OS=Salmonella typhi OX=90370 GN=rfbE PE=1 SV=2
Q57664	2.20e-38	18	352	2	303	Putative UDP-glucose 4-epimerase OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ0211 PE=3 SV=1
A0R5C5	1.12e-33	19	352	4	312	UDP-glucose 4-epimerase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=MSMEG_6142 PE=1 SV=2
P9WN67	4.36e-31	19	352	4	312	UDP-glucose 4-epimerase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=galE1 PE=1 SV=1
P9WN66	4.36e-31	19	352	4	312	UDP-glucose 4-epimerase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=galE1 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
1.000019	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002310_00986.