Reviewed, UniProtKB/Swiss-Prot Q31FY5 (FOLD2_THICR)

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
Ordered Locus Names:	Tcr_1343

Organism

Thiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]

Taxonomic identifier

317025 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira

Protein attributes

Sequence length	287 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 – 287	287	Bifunctional protein folD 2		PRO_0000268549

Sequences

	Sequence		Length	Mass (Da)
	Q31FY5-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: E897E1A0FC3CB890	FASTA	287	30,885
	10 20 30 40 50 60 MSAQVINGKV VAKTVIDRVK QRVQLRKSQG LRAPGLAVIL IGDDPASSVY VNNKKKACEE 70 80 90 100 110 120 AGLVSKSWNW PSKATQYELL ELIKQLNEDT SIDGILVQLP LPDHIDAETI IEAIHPDKDV 130 140 150 160 170 180 DGFHPYNIGR LTVRMPTLRP CTPYGCMNLL NHYDLSVKGK HAVIVGASNI VGRPMSLELL 190 200 210 220 230 240 LAGATTTVCH RFTADLQTHV SMADILVTAV GKPNFIPADW IKPGAIVVDV GINRLPDGSL 250 260 270 280 TGDVDPRARE VAAYVTPVPG GVGPMTIATL LENTLKACEI HQLGAVS

References

[1]

"The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2." Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., Hauser L.J. , Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., Zeruth G.T. PLoS Biol. 4:1-17(2006) [PubMed: 17105352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000109 Genomic DNA. Translation: ABB41938.1.
RefSeq	YP_391612.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3760705.
GenomeReviews	Gene locus Tcr_1343 in contig CP000109_GR.
KEGG	tcx:Tcr_1343.
NMPDR	fig|317025.3.peg.1283.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q31FY5.
Enzyme and pathway databases
BioCyc	TCRU317025:TCR_1343-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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOLD2_THICR

Accession

Primary (citable) accession number: Q31FY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 6, 2005
Last modified:	November 25, 2008
This is version 26 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)