P08192 (FOLC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein folC

Including the following 2 domains:

1. Folylpolyglutamate synthase
   EC=6.3.2.17
   Alternative name(s):
   Folylpoly-gamma-glutamate synthetase
   Short name=FPGS
   Tetrahydrofolylpolyglutamate synthase
   Short name=Tetrahydrofolate synthase
2. Dihydrofolate synthase
   EC=6.3.2.12

Gene names

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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

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

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.

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 Reference proteome
Gene Ontology (GO)
Biological process	10-formyltetrahydrofolate biosynthetic process Inferred from direct assay. Source: EcoliWiki folic acid biosynthetic process Inferred from direct assay. Source: EcoliWiki one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: EcoliWiki
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dihydrofolate synthase activity Inferred from direct assay. Source: EcoliWiki tetrahydrofolylpolyglutamate synthase activity Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

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

7

ATP By similarity

Amino acid modifications

Disulfide bond

354 ↔ 401

Probable

Experimental info

Sequence conflict

326

1

V → M in AAA23808. Ref.1

Sequence conflict

326

1

V → M in AAA23802. Ref.1

Sequence conflict

328

1

A → AA in AAA23966. Ref.2

Sequence conflict

391 – 392

2

DA → EP in AAA23966. Ref.2

Secondary structure

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422

Helix Strand Turn

Details...

Helix

13 – 20

8

Beta strand

23 – 27

5

Helix

33 – 42

10

Beta strand

48 – 55

8

Helix

60 – 73

14

Beta strand

78 – 81

4

Helix

89 – 92

4

Beta strand

93 – 95

3

Helix

102 – 115

14

Turn

116 – 118

3

Helix

123 – 138

16

Beta strand

141 – 146

6

Beta strand

148 – 151

4

Helix

155 – 158

4

Beta strand

162 – 166

5

Helix

174 – 177

4

Helix

181 – 186

6

Beta strand

196 – 200

5

Helix

207 – 216

10

Beta strand

219 – 223

5

Turn

224 – 226

3

Beta strand

227 – 231

5

Beta strand

236 – 240

5

Beta strand

243 – 248

6

Helix

255 – 268

14

Helix

274 – 283

10

Beta strand

289 – 294

6

Turn

295 – 297

3

Beta strand

298 – 302

5

Helix

307 – 319

13

Beta strand

326 – 330

5

Helix

338 – 346

9

Beta strand

350 – 354

5

Beta strand

359 – 362

4

Helix

365 – 372

8

Helix

381 – 391

11

Beta strand

397 – 403

7

Helix

404 – 417

14

Sequences

	Sequence		Length	Mass (Da)
	P08192 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 0C0F33D3CFB77705	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

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. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., 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.

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

NP_416818.1. NC_000913.2.

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	[»]

ProteinModelPortal

P08192.

SMR

P08192. Positions 6-419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9674N.

IntAct

P08192. 9 interactions.

MINT

MINT-1301447.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003196; EBESCP00000003196; EBESCG00000002624.
EBESCT00000016763; EBESCP00000016054; EBESCG00000015822.

GeneID

945451.

GenomeReviews

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

KEGG

ecj:JW2312.
eco:b2315.

PATRIC

32120001. VBIEscCol129921_2410.

Organism-specific databases

EchoBASE

EB0323.

EcoGene

EG10327. folC.

Phylogenomic databases

eggNOG

COG0285.

GeneTree

EBGT00050000011359.

HOGENOM

HBG744947.

OMA

AVERISI.

PhylomeDB

P08192.

ProtClustDB

PRK10846.

Enzyme and pathway databases

BioCyc

EcoCyc:FOLC-MONOMER.
MetaCyc:FOLC-MONOMER.

Gene expression databases

Genevestigator

P08192.

Family and domain databases

InterPro

IPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
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.

KO

K11754.

PANTHER

PTHR11136. Fpolygl_synthtse. 1 hit.

Pfam

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

PIRSF

PIRSF001563. Folylpolyglu_synth. 1 hit.

SUPFAM

SSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.

TIGRFAMs

TIGR01499. FolC. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

DrugBank

DB01015. Sulfamethoxazole.
DB00440. Trimethoprim.

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:	January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program