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UniProtKB/Swiss-Prot entry P08192


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

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Entry information
Entry name FOLC_ECOLI
Primary accession number P08192
Secondary accession number P78237
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 90)
Name and origin of the protein
Protein name Bifunctional protein folC
Synonyms None
Includes Folylpolyglutamate synthase
     (EC 6.3.2.17)
     (Folylpoly-gamma-glutamate synthetase)
     (FPGS)
     (Tetrahydrofolylpolyglutamate synthase)
     (Tetrahydrofolate synthase)
Dihydrofolate synthase
     (EC 6.3.2.12)
Gene name
Name: folC
Synonyms: dedC
OrderedLocusNames: b2315, JW2312
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=3040739 [NCBI, ExPASy, EBI, Israel, Japan]
Bognar A.L., Osborne C., Shane B.;
"Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene.";
J. Biol. Chem. 262:12337-12343(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3040734 [NCBI, ExPASy, EBI, Israel, Japan]
Nonet M.L., Marvel C.C., Tolan D.R.;
"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons.";
J. Biol. Chem. 262:12209-12217(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
DNA Res. 4:91-113(1997).
[4]
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).
[5]
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).
[6]
MUTAGENESIS.
DOI=10.1016/0003-9861(91)90254-G; PubMed=1989505 [NCBI, ExPASy, EBI, Israel, Japan]
Kimlova L.J., Pyne C., Keshavjee K., Huy J., Beebakhee G., Bognar A.L.;
"Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli.";
Arch. Biochem. Biophys. 284:9-16(1991).
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
M32445; AAA23808.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02808; AAA23802.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68934; AAA23966.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75375.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A65004; SYECFG.
RefSeq AP_002915.1; -.
NP_416818.1; -.
3D structure databases
PDB
1W78; X-ray; 1.82 A; A=1-422.[ExPASy / RCSB / EBI]
1W7K; X-ray; 2.10 A; A=1-422.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1W78; -.
1W7K; -.
ModBase P08192.
Protein-protein interaction databases
DIP DIP:9674N; -.
IntAct P08192; -.
Enzyme and pathway databases
BioCyc EcoCyc:FOLC-MON; -.
MetaCyc:FOLC-MON; -.
Organism-specific databases
EchoBASE EB0323; -.
EcoGene EG10327; folC.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001645; Fpolygl_synthtse.
IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
Graphical view of domain structure.
Gene3D G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
PANTHER PTHR11136; Fpolygl_synthtse; 1.
Pfam PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01499; folC; 1.
PROSITE PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PS01012; FOLYLPOLYGLU_SYNT_2; 1.
BLOCKS P08192.
ProtoNet P08192.
Genome annotation databases
GeneID 945451; -.
GenomeReviews U00096_GR; b2315.
AP009048_GR; JW2312.
KEGG ecj:JW2312; -.
eco:b2315; -.
Phylogenomic databases
HOGENOM P08192; -.
Other
DrugBank DB01015; Sulfamethoxazole.
DB00440; Trimethoprim.
Genome annotation databases
CMR P08192; b2315.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Complete proteome; Folate biosynthesis; Ligase; Multifunctional enzyme; Nucleotide-binding; One-carbon metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   422  422     Bifunctional protein folC. PRO_0000168303
NP_BIND   56    62  7     ATP (By similarity). 
DISULFID   354   401        Probable. 
CONFLICT   326   326        V -> M (in Ref. 1; AAA23808/AAA23802). 
CONFLICT   328   328        A -> AA (in Ref. 2; AAA23966). 
CONFLICT   391   392        DA -> EP (in Ref. 2; AAA23966). 
HELIX   13    20  8      
STRAND   23    27  5      
HELIX   33    42  10      
STRAND   48    55  8      
HELIX   60    73  14      
STRAND   78    81  4      
HELIX   89    92  4      
STRAND   93    95  3      
HELIX   102   115  14      
TURN   116   118  3      
HELIX   123   138  16      
STRAND   141   146  6      
STRAND   148   151  4      
HELIX   155   158  4      
STRAND   162   166  5      
HELIX   174   177  4      
HELIX   181   186  6      
STRAND   196   200  5      
HELIX   207   216  10      
STRAND   219   223  5      
TURN   224   226  3      
STRAND   227   231  5      
STRAND   236   240  5      
STRAND   243   248  6      
HELIX   255   268  14      
HELIX   274   283  10      
STRAND   289   294  6      
TURN   295   297  3      
STRAND   298   302  5      
HELIX   307   319  13      
STRAND   326   330  5      
HELIX   338   346  9      
STRAND   350   354  5      
STRAND   359   362  4      
HELIX   365   372  8      
HELIX   381   391  11      
STRAND   397   403  7      
HELIX   404   417  14      
Sequence information
Length: 422 AA [This is the length of the unprocessed precursor] Molecular weight: 45406 Da [This is the MW of the unprocessed precursor] CRC64: 0C0F33D3CFB77705 [This is a checksum on the sequence]
        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 

P08192 in FASTA format

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