Aminodeoxychorismate synthase component 1
Details
- Name
- Aminodeoxychorismate synthase component 1
- Kind
- protein
- Synonyms
- 2.6.1.85
- 4-amino-4-deoxychorismate synthase component 1
- ADC synthase
- Gene Name
- pabB
- UniProtKB Entry
- P05041Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016146|Aminodeoxychorismate synthase component 1 MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTF GKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFES LPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTL TSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAP FSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDR AENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITAQLPEQLHASDLLRA AFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIF CSAGGGIVADSQEEAEYQETFDKVNRILKQLEK
- Number of residues
- 453
- Molecular Weight
- 50969.07
- Theoretical pI
- 4.88
- GO Classification
- Functions4-amino-4-deoxychorismate synthase activity / magnesium ion binding / oxo-acid-lyase activityProcessesfolic acid biosynthetic process / tetrahydrofolate biosynthetic process
- General Function
- Oxo-acid-lyase activity
- Specific Function
- Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia.
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016147|Aminodeoxychorismate synthase component 1 (pabB) ATGAAGACGTTATCTCCCGCTGTGATTACTTTACTCTGGCGTCAGGACGCCGCTGAATTT TATTTCTCCCGCTTAAGCCACCTGCCGTGGGCGATGCTTTTACACTCCGGCTATGCCGAT CATCCGTATAGCCGCTTTGATATTGTGGTCGCCGAGCCGATTTGCACTTTAACCACTTTC GGTAAAGAAACCGTTGTTAGTGAAAGCGAAAAACGCACAACGACCACTGATGACCCGCTA CAGGTGCTCCAGCAGGTGCTGGATCGCGCAGACATTCGCCCAACGCATAACGAAGATTTG CCATTTCAGGGCGGCGCACTGGGGTTGTTTGGCTACGATCTGGGCCGCCGTTTTGAGTCA CTGCCAGAAATTGCGGAACAAGATATCGTTCTGCCGGATATGGCAGTGGGTATCTACGAT TGGGCGCTCATTGTCGACCACCAGCGTCATACAGTTTCTTTGCTGAGTCATAATGATGTC AATGCCCGTCGGGCCTGGCTGGAAAGCCAGCAATTCTCGCCGCAGGAAGATTTCACGCTC ACTTCCGACTGGCAATCCAATATGACCCGCGAGCAGTACGGCGAAAAATTTCGCCAGGTA CAGGAATATCTGCACAGCGGTGATTGCTATCAGGTGAATCTCGCCCAACGTTTTCATGCG ACCTATTCTGGCGATGAATGGCAGGCATTCCTTCAGCTTAATCAGGCCAACCGCGCGCCA TTTAGCGCTTTTTTACGTCTTGAACAGGGTGCAATTTTAAGCCTTTCGCCAGAGCGGTTT ATTCTTTGTGATAATAGTGAAATCCAGACCCGCCCGATTAAAGGCACGCTACCACGCCTG CCCGATCCTCAGGAAGATAGCAAACAAGCAGTAAAACTGGCGAACTCAGCGAAAGATCGT GCCGAAAATCTGATGATTGTCGATTTAATGCGTAATGATATCGGTCGTGTTGCCGTAGCA GGTTCGGTAAAAGTACCAGAGCTGTTCGTGGTGGAACCCTTCCCTGCCGTGCATCATCTG GTCAGCACCATAACGGCGCAACTACCAGAACAGTTACACGCCAGCGATCTGCTGCGCGCA GCTTTTCCTGGTGGCTCAATAACCGGGGCTCCGAAAGTACGGGCTATGGAAATTATCGAC GAACTGGAACCGCAGCGACGCAATGCCTGGTGCGGCAGCATTGGCTATTTGAGCTTTTGC GGCAACATGGATACCAGTATTACTATCCGCACGCTGACTGCCATTAACGGACAAATTTTC TGCTCTGCGGGCGGTGGAATTGTCGCCGATAGCCAGGAAGAAGCGGAATATCAGGAAACT TTTGATAAAGTTAATCGTATCCTGAAGCAACTGGAGAAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P05041 UniProtKB Entry Name PABB_ECOLI GenBank Protein ID 147058 GenBank Gene ID K02673 PDB ID(s) 1K0E, 1K0G KEGG ID ecj:JW1801 NCBI Gene ID 946337 - General References
- Goncharoff P, Nichols BP: Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase. J Bacteriol. 1984 Jul;159(1):57-62. [Article]
- 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 al.: 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. 1996 Dec 31;3(6):379-92. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Guttman DS, Dykhuizen DE: Detecting selective sweeps in naturally occurring Escherichia coli. Genetics. 1994 Dec;138(4):993-1003. [Article]
- Huang M, Gibson F: Biosynthesis of 4-aminobenzoate in Escherichia coli. J Bacteriol. 1970 Jun;102(3):767-73. [Article]
- Ye QZ, Liu J, Walsh CT: 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. 1990 Dec;87(23):9391-5. [Article]
- Viswanathan VK, Green JM, Nichols BP: Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J Bacteriol. 1995 Oct;177(20):5918-23. [Article]
- Rayl EA, Green JM, Nichols BP: Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association. Biochim Biophys Acta. 1996 Jun 7;1295(1):81-8. [Article]
- He Z, Stigers Lavoie KD, Bartlett PA, Toney MD: Conservation of mechanism in three chorismate-utilizing enzymes. J Am Chem Soc. 2004 Mar 3;126(8):2378-85. [Article]
- Bulloch EM, Jones MA, Parker EJ, Osborne AP, Stephens E, Davies GM, Coggins JR, Abell C: Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6s)-6-fluoroshikimate. J Am Chem Soc. 2004 Aug 18;126(32):9912-3. [Article]
- He Z, Toney MD: Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction. Biochemistry. 2006 Apr 18;45(15):5019-28. [Article]
- Parsons JF, Jensen PY, Pachikara AS, Howard AJ, Eisenstein E, Ladner JE: Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Biochemistry. 2002 Feb 19;41(7):2198-208. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Formic acid experimental, investigational unknown target Details