Species | UBA1390 sp002305315 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; UBA1390; UBA1390 sp002305315 | |||||||||||
CAZyme ID | MGYG000001728_00147 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1663; End: 4113 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH43 | 466 | 735 | 6.9e-98 | 0.9924812030075187 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08981 | GH43_Bt1873-like | 4.65e-168 | 463 | 745 | 1 | 280 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873. This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the GH43 enzymes in this family may display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
cd08175 | G1PDH | 5.38e-106 | 32 | 446 | 1 | 340 | Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner. Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer. |
COG0371 | GldA | 3.77e-64 | 35 | 409 | 11 | 359 | Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]. |
pfam13685 | Fe-ADH_2 | 4.57e-61 | 36 | 308 | 1 | 251 | Iron-containing alcohol dehydrogenase. |
cd08173 | Gro1PDH | 5.50e-55 | 35 | 383 | 5 | 321 | Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCZ48739.1 | 5.96e-110 | 464 | 757 | 4 | 295 |
QPC82363.1 | 4.47e-109 | 461 | 756 | 2 | 291 |
AFH64775.1 | 7.20e-109 | 461 | 747 | 2 | 280 |
AEI44682.1 | 7.20e-109 | 461 | 747 | 2 | 280 |
AFR28098.1 | 7.31e-108 | 463 | 756 | 1 | 293 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5C0P_A | 5.84e-66 | 457 | 753 | 15 | 298 | Thecrystal structure of endo-arabinase from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482] |
5FB3_A | 7.91e-25 | 26 | 318 | 3 | 271 | Structureof glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548],5FB3_B Structure of glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548],5FB3_C Structure of glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548],5FB3_D Structure of glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548],5FB3_E Structure of glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548],5FB3_F Structure of glycerophosphate dehydrogenase in complex with NADPH [Pyrobaculum calidifontis JCM 11548] |
4RGQ_A | 4.24e-24 | 115 | 320 | 100 | 297 | Crystalstructure of the Methanocaldococcus jannaschii G1PDH with NADPH and DHAP [Methanocaldococcus jannaschii DSM 2661],4RGQ_B Crystal structure of the Methanocaldococcus jannaschii G1PDH with NADPH and DHAP [Methanocaldococcus jannaschii DSM 2661],4RGQ_C Crystal structure of the Methanocaldococcus jannaschii G1PDH with NADPH and DHAP [Methanocaldococcus jannaschii DSM 2661],4RGQ_D Crystal structure of the Methanocaldococcus jannaschii G1PDH with NADPH and DHAP [Methanocaldococcus jannaschii DSM 2661],4RGV_A Crystal structure of the Methanocaldococcus jannaschii G1PDH [Methanocaldococcus jannaschii DSM 2661],4RGV_B Crystal structure of the Methanocaldococcus jannaschii G1PDH [Methanocaldococcus jannaschii DSM 2661] |
4RFL_A | 4.43e-24 | 115 | 320 | 103 | 300 | Crystalstructure of G1PDH with NADPH from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661],4RFL_B Crystal structure of G1PDH with NADPH from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661],4RFL_C Crystal structure of G1PDH with NADPH from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661],4RFL_D Crystal structure of G1PDH with NADPH from Methanocaldococcus jannaschii [Methanocaldococcus jannaschii DSM 2661] |
4QQS_A | 3.78e-15 | 470 | 738 | 17 | 279 | Crystalstructure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168],4QQS_B Crystal structure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9KBR3 | 4.07e-51 | 22 | 443 | 15 | 394 | Glycerol-1-phosphate dehydrogenase [NAD(P)+] OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=egsA PE=3 SV=1 |
Q65GC3 | 1.13e-47 | 22 | 446 | 15 | 385 | Glycerol-1-phosphate dehydrogenase [NAD(P)+] OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=egsA PE=3 SV=1 |
Q5WL08 | 7.19e-43 | 32 | 405 | 22 | 392 | Glycerol-1-phosphate dehydrogenase [NAD(P)+] OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=egsA PE=3 SV=1 |
A7Z7G4 | 1.00e-40 | 32 | 320 | 24 | 307 | Glycerol-1-phosphate dehydrogenase [NAD(P)+] OS=Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) OX=326423 GN=egsA PE=3 SV=1 |
B3EYN8 | 2.29e-40 | 12 | 319 | 5 | 308 | Glycerol-1-phosphate dehydrogenase [NAD(P)+] OS=Geobacillus stearothermophilus OX=1422 GN=egsA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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