Reviewed, UniProtKB/Swiss-Prot Q1AXT3 (FOLD1_RUBXD)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 1
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:	folD1
Ordered Locus Names:	Rxyl_0827

Organism

Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]

Taxonomic identifier

266117 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Rubrobacteridae › Rubrobacterales › Rubrobacterineae › Rubrobacteraceae › Rubrobacter

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate.
Pathway	One-carbon metabolism; tetrahydrofolate pathway.
Subunit structure	Homodimer By similarity.
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 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 284	284	Bifunctional protein folD 1		PRO_0000268485

Sequences

	Sequence		Length	Mass (Da)
	Q1AXT3-1 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: E077D503AF9AD8DD	FASTA	284	29,977
	10 20 30 40 50 60 MARLLDGRSV AAQIRAEVAE GVSELKRRGV PVRLDVILAG EDPASVTYVS NKRRDCAEVG 70 80 90 100 110 120 IESRLHAFPA DVPQKELLAL VERLNGDPEV SGFFIQLPLP GGVDPLPLLS AIDPSKDVDG 130 140 150 160 170 180 LSPQSAGRLA VGLPSLLPCT PHGVIQLLRR SGVGLEGREA VVVGRSNLVG KPLALLLLRE 190 200 210 220 230 240 NATVTVCHSR TRDLAGVTRR AEVLVVAAGR RGMVGAEHVR EGAVVVDVGI HRAEDGGLTG 250 260 270 280 DVRQEEVAAR AAALTPVPGG VGPMTRAMLL YNTLEAARLR EERA

References

[1]

"Complete sequence of Rubrobacter xylanophilus DSM 9941." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000386 Genomic DNA. Translation: ABG03795.1.
RefSeq	YP_643607.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4117079.
GenomeReviews	Gene locus Rxyl_0827 in contig CP000386_GR.
KEGG	rxy:Rxyl_0827.
NMPDR	fig|266117.6.peg.753.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1AXT3.
Enzyme and pathway databases
BioCyc	RXYL266117:RXYL_0827-MON.
Family and domain databases
HAMAP	MF_01576. [Tree]
InterPro	IPR016040. NAD(P)-bd. IPR000672. THF_DHase/CycOHase. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD1_RUBXD

Accession

Primary (citable) accession number: Q1AXT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 11, 2006
Last modified:	November 25, 2008
This is version 20 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)