Reviewed, UniProtKB/Swiss-Prot Q74EU7 (FOLD2_GEOSL)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 2
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:	folD2
Synonyms:	folD-2
Ordered Locus Names:	GSU0862

Organism

Geobacter sulfurreducens [Complete proteome] [HAMAP]

Taxonomic identifier

35554 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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 By similarity. HAMAP MF_01576
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 interconversion. HAMAP MF_01576
Subunit structure	Homodimer By similarity. HAMAP MF_01576
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	Complete proteome 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 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 285	285	Bifunctional protein folD 2 HAMAP MF_01576		PRO_0000268361

Sequences

	Sequence		Length	Mass (Da)
	Q74EU7-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 71C3532A95C9667A	FASTA	285	29,999
	10 20 30 40 50 60 MATIIDGKAI AEKIRADLAA QVKELQSRGI TPGLATVLVG SDPASEVYVR MKGDACNKLG 70 80 90 100 110 120 MHSVKITRPA ETTEEELLAL INELNNDPAI HGILVQLPLP PQINADRVLE AISPAKDVDG 130 140 150 160 170 180 FHPYNVGRLV TGKPTFQPCT PYGVMVMLQE AGVDLAGKEV VVVGRSNIVG KPVALMCLQR 190 200 210 220 230 240 NATVTICHSK TRDLPGRVRA ADVVIAAVGV PEMIKGDWIK EGAVVIDVGV NRVGEKKLVG 250 260 270 280 DVEFAAAAER ASAITPVPGG VGPMTITMLL HNTLEAAKMA GSGNR

References

[1]

"Genome of Geobacter sulfurreducens: metal reduction in subsurface environments." Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.L., Kolonay J.F. , Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R., Fraser C.M. Science 302:1967-1969(2003) [PubMed: 14671304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51573 / DSM 12127 / PCA.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017180 Genomic DNA. Translation: AAR34192.1.
RefSeq	NP_951919.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
SMR	Q74EU7. Positions 2-281.
ModBase	Search...
Genome annotation databases
GeneID	2687021.
GenomeReviews	Gene locus GSU0862 in contig AE017180_GR.
KEGG	gsu:GSU0862.
NMPDR	fig|243231.1.peg.857.
TIGR	GSU0862.
Phylogenomic databases
HOGENOM	HBG328751.
OMA	HSVLEKY.
Enzyme and pathway databases
BioCyc	GSUL243231:GSU_0862-MONOMER.
BRENDA	1.5.1.5. 276898. 3.5.4.9. 276898.
Family and domain databases
HAMAP	MF_01576. THF_DHG_CYH. [Tree]
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]
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.
PROSITE	PS00766. THF_DHG_CYH_1. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_GEOSL

Accession

Primary (citable) accession number: Q74EU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)