Canmetcon
Identification
Name:Para-aminobenzoate synthase component 1
Synonyms:
  • ADC synthase
  • Para-aminobenzoate synthase component I
Gene Name:pabB
Enzyme Class:
Biological Properties
General Function:Involved in biosynthetic process
Specific Function:Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+ThumbL-Glutamic acid+4-amino-4-deoxychorismate+Thumb+Thumb
Chorismate + L-Glutamine → L-Glutamic acid + 4-amino-4-deoxychorismate + L-Glutamate + 4-Amino-4-deoxychorismate
ReactionCard
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Complex Reactions:
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Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB200854-Amino-4-deoxychorismateMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB12199ChorismateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
catalytic activity
lyase activity
oxo-acid-lyase activity
Process
biosynthetic process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative biosynthetic process
folic acid and derivative metabolic process
metabolic process
Gene Properties
Blattner:b1812
Gene OrientationClockwise
Centisome Percentage:40.80
Left Sequence End1892829
Right Sequence End1894190
Gene Sequence:
>1362 bp
ATGTCTTTTGATTTAATCATTAAAAACGGCACCGTTATTTTAGAAAACGAAGCTCGCGTT
GTAGATATCGCCGTTAAAGGCGGAAAAATTGCTGCTATCGGTCAGGATCTGGGCGATGCA
AAAGAAGTTATGGATGCGTCTGGTCTGGTGGTTTCGCCGGGCATGGTTGATGCGCACACC
CATATTTCTGAACCGGGTCGTAGCCACTGGGAAGGTTATGAAACCGGTACTCGCGCAGCG
GCAAAAGGTGGTATCACCACCATGATCGAAATGCCGCTCAACCAGCTGCCTGCAACGGTT
GACCGCGCTTCAATTGAACTGAAGTTCGATGCCGCTAAAGGCAAGCTGACTATTGATGCG
GCACAACTCGGTGGCCTGGTGTCTTACAACATCGACCGTCTGCATGAGCTGGATGAAGTG
GGCGTTGTCGGCTTCAAATGCTTCGTTGCGACCTGTGGCGATCGCGGTATCGACAACGAC
TTCCGTGATGTAAACGACTGGCAGTTCTTCAAAGGTGCGCAGAAGCTGGGCGAACTGGGT
CAGCCGGTGCTGGTGCACTGCGAAAACGCGCTGATTTGTGACGAACTGGGCGAAGAAGCG
AAGCGTGAAGGTCGCGTAACCGCTCATGACTATGTGGCTTCGCGTCCGGTATTTACCGAA
GTGGAAGCAATTCGCCGCGTACTGTATCTGGCGAAAGTTGCTGGTTGCCGTCTGCACGTT
TGCCACGTCAGCAGCCCGGAAGGTGTTGAGGAAGTGACTCGTGCACGTCAGGAAGGTCAG
GACGTTACTTGTGAATCCTGCCCGCATTACTTTGTACTGGATACCGATCAGTTCGAAGAA
ATCGGTACTCTGGCGAAGTGTTCACCGCCGATCCGCGATCTGGAAAACCAGAAAGGCATG
TGGGAAAAACTGTTTAACGGTGAAATCGACTGCCTGGTTTCCGACCACTCTCCATGCCCG
CCGGAAATGAAAGCCGGTAACATCATGAAAGCATGGGGCGGTATCGCCGGTCTGCAAAGC
TGCATGGACGTGATGTTCGATGAAGCGGTACAGAAACGCGGTATGTCTCTGCCAATGTTC
GGCAAATTAATGGCGACTAACGCAGCAGATATTTTCGGTCTGCAGCAAAAAGGCCGTATC
GCCCCAGGAAAAGATGCCGACTTCGTCTTCATTCAGCCGAATAGCAGCTATGTTCTTACC
AATGACGATCTGGAATATCGCCACAAAGTCAGCCCGTATGTTGGCCGTACCATTGGCGCG
CGTATCACGAAAACCATCTTACGTGGTGATGTGATTTACGACATTGAACAGGGCTTCCCT
GTTGCGCCGAAAGGTCAATTTATCCTTAAACATCAGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:453
Protein Molecular Weight:50969
Protein Theoretical pI:5
PDB File:1K0G
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Para-aminobenzoate synthase component 1
MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTF
GKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFES
LPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTL
TSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAP
FSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDR
AENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITAQLPEQLHASDLLRA
AFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIF
CSAGGGIVADSQEEAEYQETFDKVNRILKQLEK
References
External Links:
ResourceLink
Uniprot ID:P05041
Uniprot Name:PABB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674650
PDB ID:1K0G
Ecogene ID:EG10683
Ecocyc:EG10683
ColiBase:b1812
Kegg Gene:b1812
EchoBASE ID:EB0677
CCDB:PABB_ECOLI
BacMap:16129766
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
  • Goncharoff, P., Nichols, B. P. (1984). "Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase." J Bacteriol 159:57-62. Pubmed: 6330050
  • Guttman, D. S., Dykhuizen, D. E. (1994). "Detecting selective sweeps in naturally occurring Escherichia coli." Genetics 138:993-1003. Pubmed: 7896119
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., 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., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Parsons, J. F., Jensen, P. Y., Pachikara, A. S., Howard, A. J., Eisenstein, E., Ladner, J. E. (2002). "Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes." Biochemistry 41:2198-2208. Pubmed: 11841211
  • Viswanathan, V. K., Green, J. M., Nichols, B. P. (1995). "Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli." J Bacteriol 177:5918-5923. Pubmed: 7592344
  • Ye, Q. Z., Liu, J., Walsh, C. T. (1990). "p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase." Proc Natl Acad Sci U S A 87:9391-9395. Pubmed: 2251281