Bifunctional protein folD - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P24186 (FOLD_ECOLI)

Last modified June 16, 2009. Version 76. History...

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

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Names and origin

Protein names

Recommended name:
    Bifunctional protein folD
Including the following 2 domains:
    1- Recommended name:
            Methylenetetrahydrofolate dehydrogenase
              EC=1.5.1.5
    2- Recommended name:
            Methenyltetrahydrofolate cyclohydrolase
              EC=3.5.4.9

Gene names

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

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

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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 MF_01576 5,10-methenyltetrahydrofolate + H₂O = 10-formyltetrahydrofolate. HAMAP MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate pathway. HAMAP MF_01576
Subunit structure	Homodimer. Ref.1 Ref.6
Sequence similarities	Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

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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
Gene Ontology (GO)
Biological process	folic acid and derivative 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 compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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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 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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P24186-1 [UniParc].

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

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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: 1748668] [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: 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]	"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: 10386884] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS), SUBUNIT.

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Cross-references

Sequence databases

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

AP_001176.1.
NP_415062.1.

3D structure databases

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

ModBase

Search...

Genome annotation databases

GeneID

945221.

GenomeReviews

Gene locus JW0518 in contig AP009048_GR.
Gene locus b0529 in contig U00096_GR.

KEGG

ecj:JW0518.
eco:b0529.

Organism-specific databases

EchoBASE

EB0324.

EcoGene

EG10328. folD.

CMR

Search...

Phylogenomic databases

HOGENOM

P24186.

OMA

P24186. DVVYETA.

Enzyme and pathway databases

BioCyc

EcoCyc:FOLD-MON.
MetaCyc:FOLD-MON.

Family and domain databases

HAMAP

MF_01576.
[Tree]

InterPro

IPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

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

PRINTS

PR00085. THFDHDRGNASE.

ProDom

PD002300. THFDhg/Cyc_hydro. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

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

ProtoNet

Search...

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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:	June 16, 2009
This is version 76 of the entry and version 4 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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