Species | UMGS1820 sp900769795 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1820; UMGS1820 sp900769795 | |||||||||||
CAZyme ID | MGYG000003560_00335 | |||||||||||
CAZy Family | GH105 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 12628; End: 14655 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH105 | 342 | 669 | 2.4e-68 | 0.963855421686747 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam07470 | Glyco_hydro_88 | 3.31e-47 | 312 | 671 | 1 | 343 | Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases. |
COG4225 | YesR | 5.46e-39 | 409 | 671 | 83 | 357 | Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism]. |
cd05355 | SDR_c1 | 0.007 | 192 | 253 | 9 | 85 | classical (c) SDR, subgroup 1. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QOV19133.1 | 3.02e-112 | 17 | 670 | 26 | 738 |
AGI39075.1 | 8.42e-72 | 52 | 672 | 59 | 716 |
AGC68044.1 | 8.42e-72 | 52 | 672 | 59 | 716 |
ANW98436.1 | 8.42e-72 | 52 | 672 | 59 | 716 |
QLG42731.1 | 2.12e-71 | 51 | 670 | 58 | 720 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3K11_A | 1.97e-22 | 401 | 674 | 139 | 417 | Crystalstructure of Putative glycosyl hydrolase (NP_813087.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.80 A resolution [Bacteroides thetaiotaomicron VPI-5482] |
1NC5_A | 3.41e-19 | 410 | 675 | 92 | 372 | Structureof Protein of Unknown Function of YteR from Bacillus Subtilis [Bacillus subtilis],2D8L_A Crystal Structure of Unsaturated Rhamnogalacturonyl Hydrolase in complex with dGlcA-GalNAc [Bacillus subtilis] |
2GH4_A | 1.33e-18 | 410 | 675 | 82 | 362 | ChainA, Putative glycosyl hydrolase yteR [Bacillus subtilis] |
4CE7_A | 3.45e-18 | 459 | 670 | 154 | 369 | Crystalstructure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradation [Nonlabens ulvanivorans],4CE7_B Crystal structure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradation [Nonlabens ulvanivorans],4CE7_C Crystal structure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradation [Nonlabens ulvanivorans] |
4WU0_A | 6.09e-16 | 445 | 666 | 110 | 357 | StructuralAnalysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824],4WU0_B Structural Analysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O34559 | 1.87e-18 | 410 | 675 | 92 | 372 | Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1 |
L7P9J4 | 2.03e-17 | 459 | 670 | 161 | 376 | Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Nonlabens ulvanivorans OX=906888 GN=IL45_01505 PE=1 SV=1 |
P9WF04 | 1.20e-16 | 459 | 668 | 201 | 409 | Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_28 PE=1 SV=1 |
O31521 | 1.69e-13 | 416 | 669 | 92 | 337 | Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1 |
T2KPL9 | 2.97e-13 | 459 | 619 | 159 | 331 | Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22220 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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