node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
allC | allD | b0516 | b0517 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | 0.969 |
allC | allE | b0516 | b0515 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | 0.999 |
allC | fdrA | b0516 | b0518 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | Putative NAD(P)-binding acyl-CoA synthetase; Not known; multicopy suppressor of dominant negative ftsH mutations; To E.coli YahF and some, to bacterial SucD. | 0.814 |
allC | yahG | b0516 | b0321 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | DUF1116 family protein. | 0.570 |
allC | ylbE | b0516 | b4572 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | NO-induced DUF1116 protein; To E.coli YahG. | 0.799 |
allC | ylbF | b0516 | b0520 | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | Putative anaerobic allantoin catabolic oxamate carbamoyltransferase; Putative carboxylase. | 0.686 |
allD | allC | b0517 | b0516 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | 0.969 |
allD | allE | b0517 | b0515 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | 0.997 |
allD | fdrA | b0517 | b0518 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | Putative NAD(P)-binding acyl-CoA synthetase; Not known; multicopy suppressor of dominant negative ftsH mutations; To E.coli YahF and some, to bacterial SucD. | 0.924 |
allD | yahG | b0517 | b0321 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | DUF1116 family protein. | 0.484 |
allD | ylbE | b0517 | b4572 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | NO-induced DUF1116 protein; To E.coli YahG. | 0.754 |
allD | ylbF | b0517 | b0520 | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | Putative anaerobic allantoin catabolic oxamate carbamoyltransferase; Putative carboxylase. | 0.642 |
allE | allC | b0515 | b0516 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | 0.999 |
allE | allD | b0515 | b0517 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | 0.997 |
allE | fdrA | b0515 | b0518 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Putative NAD(P)-binding acyl-CoA synthetase; Not known; multicopy suppressor of dominant negative ftsH mutations; To E.coli YahF and some, to bacterial SucD. | 0.809 |
allE | yahG | b0515 | b0321 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | DUF1116 family protein. | 0.614 |
allE | ylbE | b0515 | b4572 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | NO-induced DUF1116 protein; To E.coli YahG. | 0.814 |
allE | ylbF | b0515 | b0520 | S-ureidoglycine aminohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine. Belongs to the UGHY family. | Putative anaerobic allantoin catabolic oxamate carbamoyltransferase; Putative carboxylase. | 0.745 |
fdrA | allC | b0518 | b0516 | Putative NAD(P)-binding acyl-CoA synthetase; Not known; multicopy suppressor of dominant negative ftsH mutations; To E.coli YahF and some, to bacterial SucD. | Allantoate amidohydrolase; Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen. | 0.814 |
fdrA | allD | b0518 | b0517 | Putative NAD(P)-binding acyl-CoA synthetase; Not known; multicopy suppressor of dominant negative ftsH mutations; To E.coli YahF and some, to bacterial SucD. | Ureidoglycolate dehydrogenase; AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate. | 0.924 |