Bifunctional protein FolD - Escherichia coli (strain K12)

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P24186 (FOLD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. 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:
Bifunctional protein FolD

Including the following 2 domains:

Methylenetetrahydrofolate dehydrogenase
EC=1.5.1.5
Methenyltetrahydrofolate cyclohydrolase
EC=3.5.4.9

Gene names

Name:	folD
Synonyms:	ads
Ordered Locus Names:	b0529, JW0518

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP. Ref.1
Catalytic activity	5,10-methylenetetrahydrofolate + NADP⁺ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01576 5,10-methenyltetrahydrofolate + H₂O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01576
Subunit structure	Homodimer. Ref.1 Ref.6
Sequence similarities	Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Ligand	NADP
Molecular function	Hydrolase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	folic acid-containing compound biosynthetic process Inferred from electronic annotation. Source: InterPro histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	methenyltetrahydrofolate cyclohydrolase activity Inferred from Biological aspect of Ancestor. Source: RefGenome methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from Biological aspect of Ancestor. Source: RefGenome nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 288

287

Bifunctional protein FolD HAMAP-Rule MF_01576

PRO_0000199306

Experimental info

Sequence conflict

S → L in AAB40282. Ref.3

Sequence conflict

200

V → L in AAA23803. Ref.1

Secondary structure

288

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P24186 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 028039D7C611085D
Show »

FASTA

288

31,044

        10         20         30         40         50         60 
MAAKIIDGKT IAQQVRSEVA QKVQARIAAG LRAPGLAVVL VGSNPASQIY VASKRKACEE 

        70         80         90        100        110        120 
VGFVSRSYDL PETTSEAELL ELIDTLNADN TIDGILVQLP LPAGIDNVKV LERIHPDKDV 

       130        140        150        160        170        180 
DGFHPYNVGR LCQRAPRLRP CTPRGIVTLL ERYNIDTFGL NAVVIGASNI VGRPMSMELL 

       190        200        210        220        230        240 
LAGCTTTVTH RFTKNLRHHV ENADLLIVAV GKPGFIPGDW IKEGAIVIDV GINRLENGKV 

       250        260        270        280 
VGDVVFEDAA KRASYITPVP GGVGPMTVAT LIENTLQACV EYHDPQDE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli." D'Ari L., Rabinowitz J.C. J. Biol. Chem. 266:23953-23958(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-36, FUNCTION, SUBUNIT.
[2]	"Cloning and nucleotide sequence analysis of a novel adenine-sensitive mutation of Escherichia coli strain K-12 W3110." Yonetani Y., Sanpei G., Mizobuchi K. Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase." Shen B.W., Dyer D.H., Huang J.-Y., D'Ari L., Rabinowitz J., Stoddard B.L. Protein Sci. 8:1342-1349(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74789 Genomic DNA. Translation: AAA23803.1.
D10588 Genomic DNA. Translation: BAA01445.1.
U82664 Genomic DNA. Translation: AAB40282.1.
U00096 Genomic DNA. Translation: AAC73631.1.
AP009048 Genomic DNA. Translation: BAE76306.1.

PIR

JS0662. H64784.

RefSeq

NP_415062.1. NC_000913.2.
YP_488818.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B0A	X-ray	2.56	A	1-288	[»]

ProteinModelPortal

P24186.

SMR

P24186. Positions 2-288.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9675N.

IntAct

P24186. 4 interactions.

STRING

511145.b0529.

Proteomic databases

PaxDb

P24186.

PRIDE

P24186.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73631; AAC73631; b0529.
BAE76306; BAE76306; BAE76306.

GeneID

12933825.
945221.

KEGG

ecj:Y75_p0515.
eco:b0529.

PATRIC

32116218. VBIEscCol129921_0550.

Organism-specific databases

EchoBASE

EB0324.

EcoGene

EG10328. folD.

Phylogenomic databases

eggNOG

COG0190.

HOGENOM

HOG000218242.

K01491.

OMA

HSNVVGK.

ProtClustDB

PRK10792.

Enzyme and pathway databases

BioCyc

EcoCyc:FOLD-MONOMER.
ECOL316407:JW0518-MONOMER.
MetaCyc:FOLD-MONOMER.

SABIO-RK

P24186.

UniPathway

UPA00193.

Gene expression databases

Genevestigator

P24186.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

HAMAP

MF_01576. THF_DHG_CYH.

InterPro

IPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]

Pfam

PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]

PRINTS

PR00085. THFDHDRGNASE.

PROSITE

PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24186.

Entry information

Entry name

FOLD_ECOLI

Accession

Primary (citable) accession number: P24186
Secondary accession number(s): P77132, Q2MBQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 108 of the entry and version 4 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

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

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