Para-aminobenzoate synthase component 1 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P05041 (PABB_ECOLI)

Last modified June 16, 2009. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Para-aminobenzoate synthase component 1
    EC=2.6.1.85
Alternative name(s):
    Para-aminobenzoate synthase component I
    ADC synthase

Gene names

Name:	pabB
Ordered Locus Names:	b1812, JW1801

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine.
Catalytic activity	Chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
Subunit structure	Consists of two non-identical chains: component I catalyzes the formation of ADC by binding chorismate and ammonia; component II provides the glutamine amidotransferase activity.
Sequence similarities	Belongs to the anthranilate synthase component I family.

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Ontologies

Keywords
Biological process	Folate biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-amino-4-deoxychorismate synthase activity Inferred from electronic annotation. Source: EC oxo-acid-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Para-aminobenzoate synthase component 1

PRO_0000154136

Secondary structure

453

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P05041-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: DBF17DD5E17289D8
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FASTA

453

50,970

        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

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase." Goncharoff P., Nichols B.P. J. Bacteriol. 159:57-62(1984) [PubMed: 6330050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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." 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. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Detecting selective sweeps in naturally occurring Escherichia coli." Guttman D.S., Dykhuizen D.E. Genetics 138:993-1003(1994) [PubMed: 7896119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-377. Strain: ECOR 10, ECOR 16 and ECOR 8.
[6]	"p-aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase." Ye Q.-Z., Liu J., Walsh C.T. Proc. Natl. Acad. Sci. U.S.A. 87:9391-9395(1990) [PubMed: 2251281] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli." Viswanathan V.K., Green J.M., Nichols B.P. J. Bacteriol. 177:5918-5923(1995) [PubMed: 7592344] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes." Parsons J.F., Jensen P.Y., Pachikara A.S., Howard A.J., Eisenstein E., Ladner J.E. Biochemistry 41:2198-2208(2002) [PubMed: 11841211] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

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Cross-references

Sequence databases

K02673 Genomic DNA. Translation: AAA24266.1.
U00096 Genomic DNA. Translation: AAC74882.1.
AP009048 Genomic DNA. Translation: BAA15619.1.
U07762 Genomic DNA. Translation: AAC43282.1.
U07748 Genomic DNA. Translation: AAC43269.1.
U07749 Genomic DNA. Translation: AAC43270.1.

PIR

AGEC1. A30251.

RefSeq

AP_002431.1.
NP_416326.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K0E	X-ray	2.00	A/B	1-453	[»]
1K0G	X-ray	2.05	A/B	1-453	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10434N.

Genome annotation databases

GeneID

946337.

GenomeReviews

Gene locus JW1801 in contig AP009048_GR.
Gene locus b1812 in contig U00096_GR.

KEGG

ecj:JW1801.
eco:b1812.

Organism-specific databases

EchoBASE

EB0677.

EcoGene

EG10683. pabB.

CMR

Search...

Phylogenomic databases

HOGENOM

P05041.

OMA

P05041. QMDTSIT.

Enzyme and pathway databases

BioCyc

EcoCyc:PABASYN-COMPI-MON.
MetaCyc:PABASYN-COMPI-MON.

Family and domain databases

InterPro

IPR005801. ADC_synthase.
IPR006805. Anth_synth_I_N.
IPR019999. Anthranilate_synth_I_C.
IPR015890. Chorismate-bd_C.
IPR005802. Para-NH2Bz_synth_comp_1.
[Graphical view]

Gene3D

G3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.

PANTHER

PTHR11236. TRPE_1_chor_bd. 1 hit.

Pfam

PF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]

PRINTS

PR00095. ANTSNTHASEI.

ProDom

PD000779. Anth_synth_chor. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00553. pabB. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00634. Sulfacetamide.

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Entry information

Entry name

PABB_ECOLI

Accession

Primary (citable) accession number: P05041

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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