Q8K979 (FOLD_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein FolD

Including the following 2 domains:

1. Methylenetetrahydrofolate dehydrogenase
   EC=1.5.1.5
2. Methenyltetrahydrofolate cyclohydrolase
   EC=3.5.4.9

Gene names

Name:	folD
Ordered Locus Names:	BUsg_470

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

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-Rule MF_01576
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 By similarity. HAMAP-Rule 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-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 purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	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 HAMAP-Rule MF_01576		PRO_0000199301

Sequences

	Sequence		Length	Mass (Da)
	Q8K979 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: C9805F1577D7FB49	FASTA	285	31,609
	10 20 30 40 50 60 MSAIIIDGIK IAKKIELNLL KKIEEREKNK KRIPGLAVIL IGKNPASEIY VKRKISVCKK 70 80 90 100 110 120 VGFISKYWSF PINVDEKDIL NLIEKLNNNI NIDGILVQLP IPKQINYYKI FSSIRPDKDV 130 140 150 160 170 180 DGFHPYNTGS LCQRNPTLRA CTPKGIITML NYTKIKTHGL NAVMVGASNI VGRPMSMELL 190 200 210 220 230 240 LAGCTTTVTH RFTKNLRHHI KNADLLVVAI GKPNFLHGDW IKEGAIVIDV GINKLKDGSI 250 260 270 280 VGDVDFKSAS LKAAYITPVP GGVGPITVIT LLENTLEACE KYHEF

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM68013.1.
RefSeq	NP_660802.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K979.
SMR	Q8K979. Positions 2-284.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg470.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM68013; AAM68013; BUsg_470.
GeneID	1005697.
KEGG	bas:BUsg470.
PATRIC	21247798. VBIBucAph100086_0497.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0190.
KO	K01491.
OMA	HSNVVGK.
ProtClustDB	PRK10792.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-495-MONOMER.
UniPathway	UPA00193.
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...

Entry information

Entry name

FOLD_BUCAP

Accession

Primary (citable) accession number: Q8K979

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program