Species | UBA1067 sp900767325 | |||||||||||
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Lineage | Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; UBA1067; UBA1067 sp900767325 | |||||||||||
CAZyme ID | MGYG000003443_00658 | |||||||||||
CAZy Family | GH123 | |||||||||||
CAZyme Description | Futalosine hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6465; End: 8540 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH123 | 245 | 643 | 2.3e-130 | 0.7286245353159851 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd09008 | MTAN | 2.51e-32 | 10 | 178 | 45 | 222 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family. |
COG0775 | Pfs | 1.76e-28 | 1 | 182 | 40 | 233 | Nucleoside phosphorylase [Nucleotide transport and metabolism]. |
pfam13320 | DUF4091 | 2.08e-21 | 576 | 636 | 1 | 66 | Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important. |
pfam01048 | PNP_UDP_1 | 1.57e-20 | 11 | 179 | 49 | 231 | Phosphorylase superfamily. Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase) |
cd17877 | NP_MTAN-like | 1.66e-17 | 11 | 150 | 46 | 182 | nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QYM78770.1 | 1.41e-128 | 204 | 681 | 214 | 713 |
AYR31393.1 | 1.17e-103 | 191 | 636 | 30 | 486 |
QWO89199.1 | 6.22e-103 | 191 | 636 | 102 | 558 |
AFL77927.1 | 9.72e-103 | 266 | 636 | 174 | 540 |
QAA41011.1 | 4.96e-102 | 191 | 636 | 30 | 486 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5L7V_A | 2.20e-90 | 260 | 637 | 146 | 518 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
5L7R_A | 3.26e-90 | 260 | 637 | 161 | 533 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
5FQE_A | 3.71e-46 | 258 | 637 | 140 | 544 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
5FQG_A | 4.39e-45 | 258 | 637 | 140 | 544 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
5DK6_A | 7.29e-10 | 3 | 155 | 62 | 231 | CrystalStructure Of A 5'-methylthioadenosine/s-adenosylhomocysteine (mta/sah) Nucleosidase (mtan) From Colwellia Psychrerythraea 34h (cps_4743, Target Psi-029300) In Complex With Adenine At 2.27 A Resolution [Colwellia psychrerythraea 34H] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A6W3C9 | 6.90e-14 | 3 | 179 | 41 | 228 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Marinomonas sp. (strain MWYL1) OX=400668 GN=mtnN PE=3 SV=1 |
Q47UY5 | 1.15e-10 | 3 | 155 | 40 | 209 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Colwellia psychrerythraea (strain 34H / ATCC BAA-681) OX=167879 GN=mtnN PE=1 SV=1 |
C4LAP0 | 1.14e-08 | 1 | 155 | 38 | 204 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Tolumonas auensis (strain DSM 9187 / TA4) OX=595494 GN=mtnN PE=3 SV=1 |
P9WJM2 | 1.16e-08 | 8 | 175 | 47 | 252 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=mtnN PE=3 SV=1 |
P67657 | 1.16e-08 | 8 | 175 | 47 | 252 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=mtnN PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000029 | 0.000013 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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