HMM Summary Page: TIGR03801
| Accession | TIGR03801 |
| Name | asp_4_decarbox |
| Function | aspartate 4-decarboxylase |
| Gene Symbol | aspD |
| Trusted Cutoff | 435.10 |
| Domain Trusted Cutoff | 435.10 |
| Noise Cutoff | 213.00 |
| Domain Noise Cutoff | 213.00 |
| Isology Type | equivalog |
| EC Number | 4.1.1.12 |
| HMM Length | 521 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Amino acids and amines |
| Gene Ontology Term | GO:0006531: aspartate metabolic process biological_process |
| GO:0047688: aspartate 4-decarboxylase activity molecular_function | |
| Author | Haft DH |
| Entry Date | Aug 12 2009 10:10AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme, aspartate 4-decarboxylase (EC 4.1.1.12), removes the side-chain carboxylate from L-aspartate, converting it to L-alanine plus carbon dioxide. It is a PLP-dependent enzyme, homologous to aspartate aminotransferase (EC 2.6.1.1). |
| References | RN [1] RM PMID:19265705 RT The crystal structure of the Pseudomonas dacunhae aspartate-beta-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5'-phosphate-dependent enzyme. RA Lima S, Sundararaju B, Huang C, Khristoforov R, Momany C, Phillips RS RL J Mol Biol. 2009 Apr 24;388(1):98-108. RN [2] RM PMID:12003930 RT Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction. RA Abe K, Ohnishi F, Yagi K, Nakajima T, Higuchi T, Sano M, Machida M, Sarker RI, Maloney PC RL J Bacteriol. 2002 Jun;184(11):2906-13. DR EXPERIMENTAL; GB|AAK58507.1; Alcaligenes faecalis DR EXPERIMENTAL; GB|BAC65229.1; Pseudomonas dacunhae DR EXPERIMENTAL; GB|BAB92080.1; Tetragenococcus halophilus |
| Genome Property | GenProp0867: decarboxylation/antiport proton-motive cycle: aspartate-alanine (HMM) |