Biosynthetic arginine decarboxylase (P21170)

Identification
Name:Biosynthetic arginine decarboxylase
Synonyms:
  • ADC
Gene Name:speA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the biosynthesis of agmatine from arginine
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Arginine + 1.0Hydrogen ion ↔ 1.0Agmatine + 1.0Carbon dioxide
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Arginine ↔ 1.0Agmatine + 1.0Carbon dioxide
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Arginine + 1.0Hydrogen ion ↔ 1.0Agmatine + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Arginine → 1.0Agmatine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01432AgmatineMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00517L-ArginineMetaboCard
GO Classification:
Function
arginine decarboxylase activity
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
Process
arginine catabolic process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular amino acid metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
polyamine biosynthetic process
polyamine metabolic process
spermidine biosynthetic process
Gene Properties
Blattner:b2938
Gene OrientationCounterclockwise
Centisome Percentage:66.43
Left Sequence End3081957
Right Sequence End3083933
Gene Sequence:
>1977 bp
ATGGTATTGTTTTATCGGGCACACTGGCGCGACTATAAAAACGATCAAGTGAGGATCATG
ATGAATCTGACGACTCTGACCCACCGCGATGCGTTGTGTCTGAATGCGCGCTTTACCAGC
CGTGAAGAGGCCATCCACGCGTTGACTCAACGTCTTGCTGCTCTGGGGAAAATTTCCAGT
ACTGAGCAATTTCTGGAAGAAGTGTATCGCCGTGAAAGCCTTGGCCCGACCGCCTTAGGT
GAAGGGTTGGCTGTGCCGCATGGCAAAACTGCTGCGGTAAAAGAAGCGGCGTTTGCGGTC
GCCACACTCAGCGAGCCGCTTCAGTGGGAAGGCGTTGATGGCCCGGAAGCAGTTGATTTA
GTGGTGCTGCTGGCGATTCCCCCCAATGAAGCGGGTACTACGCATATGCAACTGCTGACA
GCGCTGACCACGCGCCTTGCGGATGATGAGATTCGGGCGCGTATACAGTCGGCGACGACG
CCTGATGAGTTGCTCTCGGCGCTGGATGACAAGGGAGGCACGCAACCTTCTGCCTCTTTT
TCCAACGCGCCAACTATCGTCTGCGTAACGGCCTGTCCGGCGGGTATTGCTCACACCTAT
ATGGCTGCGGAATATCTGGAAAAAGCCGGACGCAAACTCGGCGTAAATGTTTACGTTGAA
AAACAAGGCGCTAACGGCATTGAAGGGCGTTTAACGGCGGATCAACTCAATAGTGCAACC
GCCTGTATTTTTGCGGCTGAAGTCGCCATCAAGGAGAGTGAGCGTTTTAATGGCATTCCC
GCGCTTTCAGTGCCTGTTGCCGAGCCGATTCGCCATGCAGAAGCGTTGATCCAACAAGCG
CTTACCCTCAAGCGTAGCGATGAGACGCGTACCGTACAGCAAGATACGCAACCGGTGAAA
AGTGTCAAAACGGAGCTGAAACAGGCACTGTTGAGCGGAATCTCTTTTGCCGTACCGTTG
ATTGTCGCGGGGGGCACGGTGCTGGCGGTCGCGGTATTACTGTCGCAAATCTTCGGGCTA
CAAGATCTGTTTAATGAAGAAAACTCCTGGCTGTGGATGTACCGCAAGCTGGGCGGCGGG
CTGCTCGGAATTTTGATGGTACCGGTGCTCGCGGCCTATACCGCCTATTCTCTGGCAGAT
AAACCGGCGTTAGCGCCAGGCTTTGCGGCTGGACTTGCCGCCAACATGATCGGCTCCGGG
TTTCTCGGCGCGGTCGTTGGCGGATTGATAGCCGGTTACTTGATGCGCTGGGTGAAAAAT
CACTTGCGTCTTAGCAGTAAATTCAATGGATTCCTGACTTTTTATCTCTACCCGGTGCTC
GGTACGTTGGGAGCGGGCAGTCTGATGCTGTTTGTGGTGGGGGAACCTGTCGCCTGGATC
AATAACTCGCTTACCGCCTGGCTGAACGGTCTGTCAGGAAGTAACGCGCTGTTGCTGGGT
GCCATTCTCGGTTTTATGTGTTCCTTTGACCTTGGAGGGCCAGTGAATAAAGCCGCTTAT
GCATTCTGCCTGGGCGCAATGGCGAACGGCGTTTACGGCCCGTATGCCATTTTCGCCTCC
GTCAAAATGGTTTCGGCATTTACCGTAACCGCTTCCACGATGCTCGCACCGCGCCTGTTT
AAAGAGTTTGAAATTGAGACCGGGAAATCCACCTGGCTGTTAGGGCTGGCAGGTATTACC
GAAGGGGCGATCCCGATGGCGATTGAAGATCCGCTGCGGGTTATTGGTTCGTTTGTGCTG
GGCTCTATGGTAACGGGCGCTATTGTCGGTGCGATGAATATCGGCCTTTCGACACCCGGT
GCCGGCATTTTCTCGCTCTTTTTACTTCATGATAATGGCGCGGGCGGTGTTATGGCGGCA
ATTGGCTGGTTTGGCGCGGCATTGGTGGGGGCTGCAATCTCGACTGCAATTCTCCTGATG
TGGCGGCGTCACGCGGTTAAGCATGGCAACTATCTGACTGATGGCGTAATGCCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:658
Protein Molecular Weight:73898
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Biosynthetic arginine decarboxylase
MSDDMSMGLPSSAGEHGVLRSMQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVC
PDPDVPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDY
FLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYI
RLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEK
SKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKL
GVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITE
SGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQSMWETWQEMHEPGTRRSLREW
LHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRAHRPIIDELQER
MADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDG
DGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELS
DEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYLEDE
References
External Links:
ResourceLink
Uniprot ID:P21170
Uniprot Name:SPEA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674750
Ecogene ID:EG10959
Ecocyc:EG10959
ColiBase:b2938
Kegg Gene:b2938
EchoBASE ID:EB0952
CCDB:SPEA_ECOLI
BacMap:16130839
General Reference:
  • 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
  • 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
  • Moore, R. C., Boyle, S. M. (1990). "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli." J Bacteriol 172:4631-4640. Pubmed: 2198270
  • Szumanski, M. B., Boyle, S. M. (1992). "Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli." J Bacteriol 174:758-764. Pubmed: 1310091
  • Wu, W. H., Morris, D. R. (1973). "Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties." J Biol Chem 248:1687-1695. Pubmed: 4571773