Allantoate amidohydrolase (P77425)

Identification
Name:Allantoate amidohydrolase
Synonyms:
  • Allantoate deiminase
Gene Name:allC
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
Specific Function:Involved in the anaerobic utilization of allantoin. Converts allantoate to (S)-ureidoglycolate and ammonia
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Allantoic acid + 1.0Water ↔ 1.0Ureidoglycine + 1.0Ammonia + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Allantoic acid + 1.0Water + 2.0Hydrogen ion → 1.0Carbon dioxide + 1.0Ammonium + 1.0S-ureidoglycine
ReactionCard
Complex Reactions:
1.0Thumb+2.0Thumb+2.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Allantoic acid + 2.0Hydrogen ion + 2.0Water → 1.0Carbon dioxide + 2.0Ammonium + 1.0(S)-Ureidoglycolic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01005(S)-Ureidoglycolic acidMetaboCard
ECMDB01209Allantoic acidMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB24181S-ureidoglycineMetaboCard
ECMDB20217UreidoglycineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
protein binding
Process
metabolic process
Gene Properties
Blattner:b0516
Gene OrientationCounterclockwise
Centisome Percentage:11.71
Left Sequence End543281
Right Sequence End544516
Gene Sequence:
>1236 bp
ATGATTACACATTTCCGTCAAGCTATAGAAGAAACGCTGCCCTGGCTTTCCTCTTTTGGC
GCTGACCCAGCGGGTGGGATGACCCGTTTACTTTATTCGCCGGAATGGCTGGAAACCCAG
CAGCAATTTAAAAAAAGAATGGCAGCAAGCGGGCTGGAAACACGTTTCGATGAAGTGGGG
AATTTATACGGTCGCCTGAATGGCACCGAATATCCACAGGAAGTGGTTCTGAGCGGTTCG
CATATCGATACCGTGGTTAACGGCGGTAACCTTGACGGGCAATTCGGCGCGCTGGCGGCG
TGGCTGGCAATTGACTGGCTGAAAACGCAATACGGCGCGCCGCTACGTACGGTCGAAGTG
GTGGCGATGGCAGAAGAAGAAGGCAGCCGCTTCCCGTATGTCTTCTGGGGCAGTAAAAAT
ATTTTTGGGCTGGCGAATCCTGACGACGTGCGGAATATCTGTGATGCCAAAGGAAATAGT
TTTGTCGATGCGATGAAGGCTTGCGGATTTACTCTTCCGAACGCCCCACTAACTCCGCGT
CAGGATATTAAAGCCTTTGTTGAACTGCATATTGAACAGGGCTGTGTGCTGGAAAGTAAT
GGGCAATCAATTGGCGTGGTGAATGCAATTGTCGGGCAGCGTCGTTATACGGTAACGCTG
AACGGCGAATCAAACCATGCAGGCACCACGCCGATGGGTTATCGTCGTGATACAGTTTAC
GCTTTCAGTCGCATTTGCCATCAGTCGGTCGAAAAAGCGAAAAGGATGGGCGATCCGCTG
GTTCTGACCTTTGGCAAAGTAGAGCCGCGCCCGAATACGGTAAATGTGGTGCCGGGTAAA
ACCACGTTCACCATTGATTGTCGTCATACCGACGCTGCCGTGCTGCGCGATTTCACCCAA
CAGTTAGAAAACGACATGCGGGCGATTTGCGATGAAATGGACATTGGTATTGATATCGAT
TTATGGATGGACGAAGAACCCGTGCCGATGAATAAGGAGCTGGTCGCCACCCTGACAGAA
TTGTGTGAAAGAGAAAAACTGAATTACCGGGTGATGCACAGTGGTGCCGGGCACGACGCG
CAAATTTTCGCGCCTCGCGTACCAACCTGCATGATTTTTATCCCCAGCATCAACGGGATC
AGCCATAACCCGGCGGAACGCACCAATATTACCGACCTTGCCGAAGGGGTCAAAACGTTG
GCACTCATGCTTTATCAACTTGCCTGGCAGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:411
Protein Molecular Weight:45694
Protein Theoretical pI:5
PDB File:1Z2L
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Allantoate amidohydrolase
MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVG
NLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEV
VAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPR
QDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVY
AFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQ
QLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYRVMHSGAGHDA
QIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTLALMLYQLAWQK
References
External Links:
ResourceLink
Uniprot ID:P77425
Uniprot Name:ALLC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674654
PDB ID:1Z2L
Ecogene ID:EG13623
Ecocyc:EG13623
ColiBase:b0516
Kegg Gene:b0516
EchoBASE ID:EB3388
CCDB:ALLC_ECOLI
BacMap:16128500
General Reference:
  • Agarwal, R., Burley, S. K., Swaminathan, S. (2007). "Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics." J Mol Biol 368:450-463. Pubmed: 17362992
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cusa, E., Obradors, N., Baldoma, L., Badia, J., Aguilar, J. (1999). "Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli." J Bacteriol 181:7479-7484. Pubmed: 10601204
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553