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

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P05041 (PABB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Para-aminobenzoate synthase component 1
EC=2.6.1.85

Alternative name(s):
ADC synthase
Para-aminobenzoate synthase component I

Gene names

Name:	pabB
Ordered Locus Names:	b1812, JW1801

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

Ontologies

Keywords
Biological process	Folate biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	4-amino-4-deoxychorismate synthase activity Inferred from direct assay Ref.7. Source: EcoCyc oxo-acid-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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...

Sequences

Sequence

Length

Mass (Da)

Tools

P05041 [UniParc].

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

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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_416326.1. NC_000913.2.
YP_490073.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P05041.

SMR

P05041. Positions 3-453.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10434N.

IntAct

P05041. 5 interactions.

STRING

511145.b1812.

Proteomic databases

PaxDb

P05041.

PRIDE

P05041.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74882; AAC74882; b1812.
BAA15619; BAA15619; BAA15619.

GeneID

12931351.
946337.

KEGG

ecj:Y75_p1787.
eco:b1812.

PATRIC

32118943. VBIEscCol129921_1889.

Organism-specific databases

EchoBASE

EB0677.

EcoGene

EG10683. pabB.

Phylogenomic databases

eggNOG

COG0147.

HOGENOM

HOG000025142.

K01665.

OMA

LIVDHHK.

ProtClustDB

PRK15465.

Enzyme and pathway databases

BioCyc

EcoCyc:PABASYN-COMPI-MONOMER.
ECOL316407:JW1801-MONOMER.
MetaCyc:PABASYN-COMPI-MONOMER.

SABIO-RK

P05041.

UniPathway

UPA00077; UER00149.

Gene expression databases

Genevestigator

P05041.

Family and domain databases

Gene3D

3.60.120.10. 1 hit.

InterPro

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

Pfam

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

PRINTS

PR00095. ANTSNTHASEI.

SUPFAM

SSF56322. TRPE_1_chor_bd. 1 hit.

TIGRFAMs

TIGR00553. pabB. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00634. Sulfacetamide.

EvolutionaryTrace

P05041.

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:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents