NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.;
"Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.

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.
CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H₂O = 10-formyltetrahydrofolate.
PATHWAY: One-carbon metabolism; tetrahydrofolate pathway .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000738; ABR60928.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001327763.1; -.

3D structure databases

ModBase

A6UB98.

Ontologies

GO:0004477;	Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004488;	Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01576; -; 1.
PBIL [Tree]

InterPro

IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00085; THFDHDRGNASE.

ProDom

PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.

BLOCKS

A6UB98.

Genome annotation databases

GeneID

5322955; -.

GenomeReviews

CP000738_GR; Smed_2095.

KEGG

smd:Smed_2095; -.

CMR

A6UB98; Smed_2095.

Other

ProtoNet

A6UB98.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 297`	`297`		`Bifunctional protein folD 2.`	`PRO_0000340598`

Sequence information

Length: 297 AA [This is the length of the unprocessed precursor]

Molecular weight: 31345 Da [This is the MW of the unprocessed precursor]

CRC64: 5F82D79C48EEAE01 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGMDRIADRA IIDGKRFAAG LLDDITARVK KLEEETGQVP GLAVVLVGED PASRVYVGSK 

        70         80         90        100        110        120 
HRQTLAAGIA SFKYELPAET TQEELMALID RLNVDPAVHG ILVQLPLPAH LDANAVIQEI 

       130        140        150        160        170        180 
NPNKDVDGFH ISNAGRLATG QPAFVPCTPL GCLLLLKDRL GANLSGLHAV VLGKSNIVGR 

       190        200        210        220        230        240 
PMVQLLLAES CTVTIAHSRT RNAPELCREA DILIVAVGRP GLVRGDWIKP GAVVIDVGIN 

       250        260        270        280        290 
RVEAEGKSRI VGDVAFEEAG HAGAITPVPG GVGPMTIACL LSNTLTAFCR QHAVNID

A6UB98 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools