Reviewed, UniProtKB/Swiss-Prot Q5LNV2 (FOLD1_SILPO)

Names and origin

Protein names

Recommended name:
    Bifunctional protein folD 1/3
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:	SPO1559
AND
Name:	folD3
Ordered Locus Names:	SPO3101

Organism

Silicibacter pomeroyi [Complete proteome] [HAMAP]

Taxonomic identifier

89184 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	296 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. HAMAP MF_01576 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP MF_01576
Pathway	One-carbon metabolism; tetrahydrofolate pathway. HAMAP MF_01576
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 – 296	296	Bifunctional protein folD 1/3 HAMAP MF_01576		PRO_0000268501

Sequences

	Sequence		Length	Mass (Da)
	Q5LNV2-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: E8331BCC13CE786C	FASTA	296	30,926
	10 20 30 40 50 60 MAATVIDGKA FAARIRGQVA EHVAELKAGH GITPGLAVVL VGEDPASQVY VRSKGKQTVE 70 80 90 100 110 120 VGMNSYEHKL DADTSEADLL ALIDRLNGDP DVHGILVQLP LPGHLDEDLV INAIDPAKDV 130 140 150 160 170 180 DGFHISNVGL LGTGQKSMVP CTPLGCLMML RDHHGSLSGM DAVVIGRSNI VGKPMAQLLL 190 200 210 220 230 240 GDSCTVTIAH SRTKDLADVV RRADIVVAAV GRPEMVPGDW IKPGATVIDV GINRIERDGK 250 260 270 280 290 TRLVGDVHYD SCAQVAGAIT PVPGGVGPMT IACLLANTLT ACTRANKLTE PDGLTP

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
EMBLGenBankDDBJ	CP000031 Genomic DNA. Translation: AAV96336.1. CP000031 Genomic DNA. Translation: AAV94846.1.
RefSeq	YP_166800.1. YP_168304.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3193798. 3194901.
GenomeReviews	Gene locus SPO1559 in contig CP000031_GR. Gene locus SPO3101 in contig CP000031_GR.
KEGG	sil:SPO1559. sil:SPO3101.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LNV2.
OMA	Q5LNV2. MQIIDGK.
Enzyme and pathway databases
BioCyc	SPOM246200:SPO_1559-MON. SPOM246200:SPO_3101-MON.
BRENDA	1.5.1.5. 278247. 3.5.4.9. 278247.
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...

Entry information

Entry name

FOLD1_SILPO

Accession

Primary (citable) accession number: Q5LNV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	February 1, 2005
Last modified:	June 16, 2009
This is version 32 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)