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B6db families: 4.1.1.19.1

4.1.1.19 1
Activity 4.1.1.19
Description Arginine decarboxylase (family 1)
Notes This family includes plant and proteobacterial (biosynthetic) arginine decarboxylases, which are fold-type III enzymes.
In contrast, the Escherichia coli biodegradative arginine decarboxylase and other bacterial arginine decarboxylases are fold-type I enzymes and have been grouped in family 4.1.1.19_2.
PDB 3NZP;3NZQ;
PLP Fold Type III
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type III

Number of sequences 29
Sequences in seed alignment
ViridiplantaeAEQ02349 (Erythroxylum coca);
BacteriaSPA1_SYNY3 (Synechocystis sp. (strain PCC 6803)); AAF09826 (Deinococcus radiodurans); CAE08874 (Synechococcus sp. WH 8102); AAD07486 (Helicobacter pylori 26695); BAC92011 (Gloeobacter violaceus); BAC09359 (Thermosynechococcus elongatus); NP_487441 (Nostoc sp. PCC 7120); SPEA_ECOLI (Escherichia coli); AAS81619 (Thermus thermophilus); Q9PPF5 (Campylobacter jejuni); YP_009641 (Desulfovibrio vulgaris); NP_233201 (Vibrio cholerae); NP_284719 (Neisseria meningitidis); ZP_00066511 (Microbulbifer degradans); NP_812306 (Bacteroides thetaiotaomicron); AAM38760 (Xanthomonas axonopodis); AAQ60544 (Chromobacterium violaceum);
ViridiplantaeCAE02767 (Oryza sativa); CDM81060 (Triticum aestivum); SPE1_ARATH (Arabidopsis thaliana); SPE1_PEA (Pisum sativum); SPE1_SOYBN (Glycine max); SPE1_DIACA (Dianthus caryophyllus); AAR08422 (Pringlea antiscorbutica); SPE2_ARATH (Arabidopsis thaliana); SPE1_BRAJU (Brassica juncea); SPE1_AVESA (Avena sativa); SPE1_ORYSA (Oryza sativa);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence SPE1_ARATH
Domain interval 107-384
Catalytic site 136 K
 
References
 Alam M, Srivastava A, Dutta A, Sau AK (2018) Biochemical and biophysical studies of Helicobacter pylori arginine decarboxylase, an enzyme important for acid adaptation in host IUBMB Life 70 658-669.

 Docimo T, Reichelt M, Schneider B, Kai M, Kunert G, Gershenzon J, D'Auria JC. (2012) The first step in the biosynthesis of cocaine in Erythroxylum coca: the characterization of arginine and ornithine decarboxylases. Plant Mol Biol. 78 599-615.

 Forouhar F1, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L. (2010) Structures of bacterial biosynthetic arginine decarboxylases. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66 1562-6.

 Hanfrey, C.; Sommer, S.; Mayer, M.J., Burtin, D., Michael, A.J. (2001) Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity Plant J 27 551-60.

 Sekowska, A.; Bertin, P.; Danchin, A. (1998) Characterization of polyamine synthesis pathway in Bacillus subtilis 168 Mol Microbiol 29 851-8.

 Bell, E.; Malmberg, R.L. (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing Mol Gen Genet 224 431-6.

 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 4631-40.

Articles on 4.1.1.19.1
last changed 2018/05/23 15:11

B6db families