Q5LT54 (FOLD2_SILPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein FolD 2

Including the following 2 domains:

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

Gene names

Name:	folD2
Ordered Locus Names:	SPO1560

Organism

Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]

Taxonomic identifier

246200 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	292 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-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 electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: EC methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC 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
	Chain	1 – 292	292	Bifunctional protein FolD 2 HAMAP MF_01576		PRO_0000268502

Sequences

	Sequence		Length	Mass (Da)
	Q5LT54 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 9517A3C932983280	FASTA	292	30,883
	10 20 30 40 50 60 MSTVADTRLL PGKPVRARIL SEVSAYVNQV GRIGKLVSIS IGNVPEVAVY VRNQARAASA 70 80 90 100 110 120 VGVPFDQQLW DRSISQEVCQ SLIREMNDDP DVLGIILQRP VPDHINVRAL QAAIHPLKDV 130 140 150 160 170 180 EGMNPASIGN IVYNDVAMAP CTAAAAIELI RETGLSMAGL EVVMVGHSEI VGKPVAMMLM 190 200 210 220 230 240 AEGATVTVCH HMTRSDAMHS RRADVVVVAV GKAHLIGPDM IKPGAVVIDI GINHVPGPDG 250 260 270 280 290 PVVVGDVQTD AVKDVAGWIT PVPGGVGLVT VAILLRNAIR AHQQQRAAGW IH

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000031 Genomic DNA. Translation: AAV94847.1.
RefSeq	YP_166801.1. NC_003911.11.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ProteinModelPortal	Q5LT54.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3193492.
GenomeReviews	Gene locus SPO1560 in contig CP000031_GR.
KEGG	sil:SPO1560.
NMPDR	fig|246200.3.peg.1970.
PATRIC	23376439. VBIRuePom114501_1584.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG328751.
OMA	SIGNIVY.
ProtClustDB	CLSK506682.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_1560-MONOMER.
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. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01491.
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. False negative. PS00767. THF_DHG_CYH_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_SILPO

Accession

Primary (citable) accession number: Q5LT54

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	February 1, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program