NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)⁺ = 5,10-methylenetetrahydrofolate + NAD(P)H.
COFACTOR: FAD (By similarity).
PATHWAY: One-carbon metabolism; tetrahydrofolate pathway .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the methylenetetrahydrofolate reductase 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

AE005674; AAN45452.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP18748.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_709745.1; -.
NP_838937.1; -.

3D structure databases

SMR

P0AEZ2; 3-294.

ModBase

P0AEZ2.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN45452.1-MON; -.

Ontologies

GO:0004489;	Molecular function: methylenetetrahydrofolate reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0009086;	Biological process: methionine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003171; Mehydrof_redctse.
IPR004620; MTHF_reductase_bac.
Graphical view of domain structure.

Pfam

PF02219; MTHFR; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00676; fadh2; 1.

Genome annotation databases

GeneID

1027371; -.
1079941; -.

GenomeReviews

AE005674_GR; SF4019.
AE014073_GR; S3728.

KEGG

sfl:SF4019; -.
sfx:S3728; -.

Phylogenomic databases

HOGENOM

P0AEZ2; -.

Genome annotation databases

CMR

P0AEZ2; SF4019.

Other

ProtoNet

P0AEZ2.

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; Methionine biosynthesis; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 296`	`296`		`5,10-methylenetetrahydrofolate reductase.`	`PRO_0000190265`

Sequence information

Length: 296 AA [This is the length of the unprocessed precursor]

Molecular weight: 33103 Da [This is the MW of the unprocessed precursor]

CRC64: B702702D2BE9521E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFFHASQRD ALNQSLAEVQ GQINVSFEFF PPRTSEMEQT LWNSIDRLSS LKPKFVSVTY 

        70         80         90        100        110        120 
GANSGERDRT HSIIKGIKDR TGLEAAPHLT CIDATPDELR TIARDYWNNG IRHIVALRGD 

       130        140        150        160        170        180 
LPPGSGKPEM YASDLVTLLK EVADFDISVA AYPEVHPEAK SAQADLLNLK RKVDAGANRA 

       190        200        210        220        230        240 
ITQFFFDVES YLRFRDRCVS AGIDVEIIPG ILPVSNFKQA KKFADMTNVR IPAWMAQMFD 

       250        260        270        280        290 
GLDDDAETRK LVGANIAMDM VKILSREGVK DFHFYTLNRA EMSYAICHTL GVRPGL

P0AEZ2 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