Identification
Name:Glutamate decarboxylase beta
Synonyms:
  • GAD-beta
Gene Name:gadB
Enzyme Class:
Biological Properties
General Function:Involved in glutamate decarboxylase activity
Specific Function:Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria
Cellular Location:Cytoplasm. Membrane.
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb1.0Hypotaurine+1.0Thumb+1.0Thumb
1.0Cysteic acid+1.0Thumb1.0Thumb+1.0Thumb
1.0Cysteic acid + 1.0Cysteic acid → 1.0Taurine + 1.0Carbon dioxide
ReactionCard
1.0L-Glutamic acid+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB009963-SulfinoalanineMetaboCard
ECMDB121614-(Glutamylamino) butanoateMetaboCard
ECMDB00510Aminoadipic acidMetaboCard
ECMDB00056beta-AlanineMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB02757Cysteic acidMetaboCard
ECMDB04017gamma-Aminobutyric acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00965HypotaurineMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00251TaurineMetaboCard
GO Classification:
Function
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
cofactor binding
glutamate decarboxylase activity
lyase activity
pyridoxal phosphate binding
Process
carboxylic acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamate metabolic process
glutamine family amino acid metabolic process
metabolic process
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Blattner:b1493
Gene OrientationCounterclockwise
Centisome Percentage:33.81
Left Sequence End1568669
Right Sequence End1570069
Gene Sequence:
>1401 bp
ATGGATAAGAAGCAAGTAACGGATTTAAGGTCGGAACTACTCGATTCACGTTTTGGTGCG
AAGTCTATTTCCACTATCGCAGAATCAAAACGTTTTCCGCTGCACGAAATGCGCGACGAT
GTCGCATTCCAGATTATCAATGACGAATTATATCTTGATGGCAACGCTCGTCAGAACCTG
GCCACTTTCTGCCAGACCTGGGACGACGAAAATGTCCACAAATTGATGGATTTATCCATT
AACAAAAACTGGATCGACAAAGAAGAATATCCGCAATCCGCAGCCATCGACCTGCGTTGC
GTAAATATGGTTGCCGATCTGTGGCATGCGCCTGCGCCGAAAAATGGTCAGGCCGTTGGC
ACCAACACCATTGGTTCTTCCGAGGCCTGTATGCTCGGCGGGATGGCGATGAAATGGCGT
TGGCGCAAGCGTATGGAAGCTGCAGGCAAACCAACGGATAAACCAAACCTGGTGTGCGGT
CCGGTACAAATCTGCTGGCATAAATTCGCCCGCTACTGGGATGTGGAGCTGCGTGAGATC
CCTATGCGCCCCGGTCAGTTGTTTATGGACCCGAAACGCATGATTGAAGCCTGTGACGAA
AACACCATCGGCGTGGTGCCGACTTTCGGCGTGACCTACACTGGTAACTATGAGTTCCCA
CAACCGCTGCACGATGCGCTGGATAAATTCCAGGCCGATACCGGTATCGACATCGACATG
CACATCGACGCTGCCAGCGGTGGCTTCCTGGCACCGTTCGTCGCCCCGGATATCGTCTGG
GACTTCCGCCTGCCGCGTGTGAAATCGATCAGTGCTTCAGGCCATAAATTCGGTCTGGCT
CCGCTGGGCTGCGGCTGGGTTATCTGGCGTGACGAAGAAGCGCTGCCGCAGGAACTGGTG
TTCAACGTTGACTACCTGGGTGGTCAAATTGGTACTTTTGCCATCAACTTCTCCCGCCCG
GCGGGTCAGGTAATTGCACAGTACTATGAATTCCTGCGCCTCGGTCGTGAAGGCTATACC
AAAGTACAGAACGCCTCTTACCAGGTTGCCGCTTATCTGGCGGATGAAATCGCCAAACTG
GGGCCGTATGAGTTCATCTGTACGGGTCGCCCGGACGAAGGCATCCCGGCGGTTTGCTTC
AAACTGAAAGATGGTGAAGATCCGGGATACACCCTGTATGACCTCTCTGAACGTCTGCGT
CTGCGCGGCTGGCAGGTTCCGGCCTTCACTCTCGGCGGTGAAGCCACCGACATCGTGGTG
ATGCGCATTATGTGTCGTCGCGGCTTCGAAATGGACTTTGCTGAACTGTTGCTGGAAGAC
TACAAAGCCTCCCTGAAATATCTCAGCGATCACCCGAAACTGCAGGGTATTGCCCAACAG
AACAGCTTTAAACATACCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:466
Protein Molecular Weight:52668
Protein Theoretical pI:5
PDB File:1PMO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutamate decarboxylase beta
MDKKQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNL
ATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVG
TNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREI
PMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDM
HIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELV
FNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKL
GPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVV
MRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
References
External Links:
ResourceLink
Uniprot ID:P69910
Uniprot Name:DCEB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742450
PDB ID:1PMO
Ecogene ID:EG11490
Ecocyc:EG11490
ColiBase:b1493
Kegg Gene:b1493
EchoBASE ID:EB1453
CCDB:DCEB_ECOLI
BacMap:16129452
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Capitani, G., De Biase, D., Aurizi, C., Gut, H., Bossa, F., Grutter, M. G. (2003). "Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase." EMBO J 22:4027-4037. Pubmed: 12912902
  • De Biase, D., Tramonti, A., Bossa, F., Visca, P. (1999). "The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system." Mol Microbiol 32:1198-1211. Pubmed: 10383761
  • 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
  • Ma, Z., Gong, S., Richard, H., Tucker, D. L., Conway, T., Foster, J. W. (2003). "GadE (YhiE) activates glutamate decarboxylase-dependent acid resistance in Escherichia coli K-12." Mol Microbiol 49:1309-1320. Pubmed: 12940989
  • Ma, Z., Richard, H., Tucker, D. L., Conway, T., Foster, J. W. (2002). "Collaborative regulation of Escherichia coli glutamate-dependent acid resistance by two AraC-like regulators, GadX and GadW (YhiW)." J Bacteriol 184:7001-7012. Pubmed: 12446650
  • Masuda, N., Church, G. M. (2002). "Escherichia coli gene expression responsive to levels of the response regulator EvgA." J Bacteriol 184:6225-6234. Pubmed: 12399493
  • Masuda, N., Church, G. M. (2003). "Regulatory network of acid resistance genes in Escherichia coli." Mol Microbiol 48:699-712. Pubmed: 12694615
  • Smith, D. K., Kassam, T., Singh, B., Elliott, J. F. (1992). "Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci." J Bacteriol 174:5820-5826. Pubmed: 1522060
  • Tramonti, A., John, R. A., Bossa, F., De Biase, D. (2002). "Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli." Eur J Biochem 269:4913-4920. Pubmed: 12383249
  • Tramonti, A., Visca, P., De Canio, M., Falconi, M., De Biase, D. (2002). "Functional characterization and regulation of gadX, a gene encoding an AraC/XylS-like transcriptional activator of the Escherichia coli glutamic acid decarboxylase system." J Bacteriol 184:2603-2613. Pubmed: 11976288
  • Turlin, E., Gasser, F., Biville, F. (1996). "Sequence and functional analysis of an Escherichia coli DNA fragment able to complement pqqE and pqqF mutants from Methylobacterium organophilum." Biochimie 78:823-831. Pubmed: 9116051
  • Waterman, S. R., Small, P. L. (2003). "Transcriptional expression of Escherichia coli glutamate-dependent acid resistance genes gadA and gadBC in an hns rpoS mutant." J Bacteriol 185:4644-4647. Pubmed: 12867478
  • Yoshida, T., Ueguchi, C., Yamada, H., Mizuno, T. (1993). "Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant." Mol Gen Genet 237:113-122. Pubmed: 8455549
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842