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UniProtKB/Swiss-Prot entry P05041


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PABB_ECOLI
Primary accession number P05041
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 88)
Name and origin of the protein
Protein name Para-aminobenzoate synthase component 1
Synonyms EC 2.6.1.85
Para-aminobenzoate synthase component I
ADC synthase
Gene name
Name: pabB
OrderedLocusNames: b1812, JW1801
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6330050 [NCBI, ExPASy, EBI, Israel, Japan]
Goncharoff P., Nichols B.P.;
"Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase.";
J. Bacteriol. 159:57-62(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., 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., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"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(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, 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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-377.
STRAIN=ECOR 10, ECOR 16, and ECOR 8;
PubMed=7896119 [NCBI, ExPASy, EBI, Israel, Japan]
Guttman D.S., Dykhuizen D.E.;
"Detecting selective sweeps in naturally occurring Escherichia coli.";
Genetics 138:993-1003(1994).
[6]
CHARACTERIZATION.
PubMed=2251281 [NCBI, ExPASy, EBI, Israel, Japan]
Ye Q.-Z., Liu J., Walsh C.T.;
"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(1990).
[7]
CHARACTERIZATION.
PubMed=7592344 [NCBI, ExPASy, EBI, Israel, Japan]
Viswanathan V.K., Green J.M., Nichols B.P.;
"Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli.";
J. Bacteriol. 177:5918-5923(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1021/bi015791b; PubMed=11841211 [NCBI, ExPASy, EBI, Israel, Japan]
Parsons J.F., Jensen P.Y., Pachikara A.S., Howard A.J., Eisenstein E., Ladner J.E.;
"Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes.";
Biochemistry 41:2198-2208(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02673; AAA24266.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74882.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15619.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07762; AAC43282.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07748; AAC43269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07749; AAC43270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A30251; AGEC1.
RefSeq AP_002431.1; -.
NP_416326.1; -.
3D structure databases
PDB
1K0E; X-ray; 2.00 A; A/B=1-453.[ExPASy / RCSB / EBI]
1K0G; X-ray; 2.05 A; A/B=1-453.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1K0E; -.
1K0G; -.
ModBase P05041.
Protein-protein interaction databases
DIP DIP:10434N; -.
Enzyme and pathway databases
BioCyc EcoCyc:PABASYN-COMPI-MON; -.
MetaCyc:PABASYN-COMPI-MON; -.
Organism-specific databases
EchoBASE EB0677; -.
EcoGene EG10683; pabB.
Ontologies
GO
GO:0016740; Molecular function: transferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0046656; Biological process: folic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006805; Anth_synth_I_N.
IPR015890; Chorismate-bd_C.
IPR005802; Para-NH2Bz_synth_comp_1.
IPR005801; TRPE_1_chor_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
PANTHER PTHR11236; TRPE_1_chor_bd; 1.
Pfam PF04715; Anth_synt_I_N; 1.
PF00425; Chorismate_bind; 1.
Pfam graphical view of domain structure.
PRINTS PR00095; ANTSNTHASEI.
ProDom PD000779; Anth_synth_chor; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00553; pabB; 1.
BLOCKS P05041.
ProtoNet P05041.
Genome annotation databases
GeneID 946337; -.
GenomeReviews U00096_GR; b1812.
AP009048_GR; JW1801.
KEGG ecj:JW1801; -.
eco:b1812; -.
Phylogenomic databases
HOGENOM P05041; -.
Other
DrugBank DB00634; Sulfacetamide.
Genome annotation databases
CMR P05041; b1812.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Folate biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   453  453     Para-aminobenzoate synthase component 1. PRO_0000154136
STRAND   7    11  5      
HELIX   17    22  6      
TURN   23    27  5      
STRAND   32    35  4      
STRAND   46    50  5      
STRAND   54    60  7      
STRAND   63    68  6      
STRAND   71    75  5      
HELIX   79    89  11      
STRAND   104   110  7      
HELIX   112   117  6      
STRAND   133   146  14      
TURN   147   150  4      
STRAND   151   158  8      
HELIX   160   169  10      
STRAND   185   188  4      
HELIX   190   205  16      
STRAND   212   224  13      
HELIX   226   237  12      
STRAND   241   246  6      
STRAND   251   256  6      
STRAND   261   264  4      
STRAND   267   270  4      
STRAND   273   278  6      
TURN   297   301  5      
HELIX   302   314  13      
TURN   315   317  3      
STRAND   324   333  10      
STRAND   335   347  13      
HELIX   354   361  8      
HELIX   365   367  3      
HELIX   372   382  11      
STRAND   383   385  3      
TURN   388   391  4      
STRAND   392   398  7      
STRAND   403   406  4      
STRAND   410   415  6      
STRAND   418   427  10      
HELIX   433   451  19      
Sequence information
Length: 453 AA [This is the length of the unprocessed precursor] Molecular weight: 50970 Da [This is the MW of the unprocessed precursor] CRC64: DBF17DD5E17289D8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTLSPAVIT LLWRQDAAEF YFSRLSHLPW AMLLHSGYAD HPYSRFDIVV AEPICTLTTF 

        70         80         90        100        110        120 
GKETVVSESE KRTTTTDDPL QVLQQVLDRA DIRPTHNEDL PFQGGALGLF GYDLGRRFES 

       130        140        150        160        170        180 
LPEIAEQDIV LPDMAVGIYD WALIVDHQRH TVSLLSHNDV NARRAWLESQ QFSPQEDFTL 

       190        200        210        220        230        240 
TSDWQSNMTR EQYGEKFRQV QEYLHSGDCY QVNLAQRFHA TYSGDEWQAF LQLNQANRAP 

       250        260        270        280        290        300 
FSAFLRLEQG AILSLSPERF ILCDNSEIQT RPIKGTLPRL PDPQEDSKQA VKLANSAKDR 

       310        320        330        340        350        360 
AENLMIVDLM RNDIGRVAVA GSVKVPELFV VEPFPAVHHL VSTITAQLPE QLHASDLLRA 

       370        380        390        400        410        420 
AFPGGSITGA PKVRAMEIID ELEPQRRNAW CGSIGYLSFC GNMDTSITIR TLTAINGQIF 

       430        440        450 
CSAGGGIVAD SQEEAEYQET FDKVNRILKQ LEK 

P05041 in FASTA format

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