Bifunctional protein folC - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P08192 (FOLC_ECOLI)

Last modified February 9, 2010. Version 103. History...

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

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Names and origin

Protein names

Recommended name:
    Bifunctional protein folC
Including the following 2 domains:
    1- Recommended name:
            Folylpolyglutamate synthase
              EC=6.3.2.17
        Alternative name(s):
            Folylpoly-gamma-glutamate synthetase
              Short name=FPGS
            Tetrahydrofolylpolyglutamate synthase
              Short name=Tetrahydrofolate synthase
    2- Recommended name:
            Dihydrofolate synthase
              EC=6.3.2.12

Gene names

Name:	folC
Synonyms:	dedC
Ordered Locus Names:	b2315, JW2312

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	422 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Conversion of folates to polyglutamate derivatives.
Catalytic activity	ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Subunit structure	Monomer.
Sequence similarities	Belongs to the folylpolyglutamate synthase family.

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Ontologies

Keywords
Biological process	Folate biosynthesis One-carbon metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	10-formyltetrahydrofolate biosynthetic process Inferred from direct assay. Source: UniProtKB folic acid biosynthetic process Inferred from direct assay. Source: UniProtKB one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dihydrofolate synthase activity Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct tetrahydrofolylpolyglutamate synthase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
b1588	Q8KS88	1	EBI-550459,EBI-878487	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Bifunctional protein folC

PRO_0000168303

Regions

Nucleotide binding

56 – 62

ATP By similarity

Amino acid modifications

Disulfide bond

354 ↔ 401

Probable

Experimental info

Sequence conflict

326

V → M in AAA23808. Ref.1

Sequence conflict

326

V → M in AAA23802. Ref.1

Sequence conflict

328

A → AA in AAA23966. Ref.2

Sequence conflict

391 – 392

DA → EP in AAA23966. Ref.2

Secondary structure

422

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P08192-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 0C0F33D3CFB77705
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FASTA

422

45,406

        10         20         30         40         50         60 
MIIKRTPQAA SPLASWLSYL ENLHSKTIDL GLERVSLVAA RLGVLKPAPF VFTVAGTNGK 

        70         80         90        100        110        120 
GTTCRTLESI LMAAGYKVGV YSSPHLVRYT ERVRVQGQEL PESAHTASFA EIESARGDIS 

       130        140        150        160        170        180 
LTYFEYGTLS ALWLFKQAQL DVVILEVGLG GRLDATNIVD ADVAVVTSIA LDHTDWLGPD 

       190        200        210        220        230        240 
RESIGREKAG IFRSEKPAIV GEPEMPSTIA DVAQEKGALL QRRGVEWNYS VTDHDWAFSD 

       250        260        270        280        290        300 
AHGTLENLPL PLVPQPNAAT ALAALRASGL EVSENAIRDG IASAILPGRF QIVSESPRVI 

       310        320        330        340        350        360 
FDVAHNPHAA EYLTGRMKAL PKNGRVLAVI GMLHDKDIAG TLAWLKSVVD DWYCAPLEGP 

       370        380        390        400        410        420 
RGATAEQLLE HLGNGKSFDS VAQAWDAAMA DAKAEDTVLV CGSFHTVAHV MEVIDARRSG 


GK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene." Bognar A.L., Osborne C., Shane B. J. Biol. Chem. 262:12337-12343(1987) [PubMed: 3040739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." Nonet M.L., Marvel C.C., Tolan D.R. J. Biol. Chem. 262:12209-12217(1987) [PubMed: 3040734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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.
[6]	"Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli." Kimlova L.J., Pyne C., Keshavjee K., Huy J., Beebakhee G., Bognar A.L. Arch. Biochem. Biophys. 284:9-16(1991) [PubMed: 1989505] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32445 Genomic DNA. Translation: AAA23808.1.
J02808 Genomic DNA. Translation: AAA23802.1.
M68934 Genomic DNA. Translation: AAA23966.1.
U00096 Genomic DNA. Translation: AAC75375.1.
AP009048 Genomic DNA. Translation: BAA16164.1.

PIR

SYECFG. A65004.

RefSeq

AP_002915.1.
NP_416818.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W78	X-ray	1.82	A	1-422	[»]
1W7K	X-ray	2.10	A	1-422	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9674N.

IntAct

P08192. 9 interactions.

STRING

P08192.

Genome annotation databases

GeneID

945451.

GenomeReviews

Gene locus JW2312 in contig AP009048_GR.
Gene locus b2315 in contig U00096_GR.

KEGG

ecj:JW2312.
eco:b2315.

Organism-specific databases

EchoBASE

EB0323.

EcoGene

EG10327. folC.

CMR

Search...

Phylogenomic databases

eggNOG

COG0285.

HOGENOM

HBG744947.

OMA

SIHPTEI.

Enzyme and pathway databases

BioCyc

EcoCyc:FOLC-MONOMER.
ECOL168927:B2315-MONOMER.
MetaCyc:FOLC-MONOMER.

Gene expression databases

Genevestigator

P08192.

Family and domain databases

InterPro

IPR018109. Folylpolyglutamate_synth_CS.
IPR001645. Fpolygl_synthtse.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]

Gene3D

G3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.

PANTHER

PTHR11136. Fpolygl_synthtse. 1 hit.

Pfam

PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01499. folC. 1 hit.

PROSITE

PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01015. Sulfamethoxazole.
DB00440. Trimethoprim.

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Entry information

Entry name

FOLC_ECOLI

Accession

Primary (citable) accession number: P08192
Secondary accession number(s): P78237

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 103 of the entry and version 2 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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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents