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Protein

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial

Gene

Nmdmc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

May play a role in spermatogenesis.

Catalytic activityi

5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH.
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.

Cofactori

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB
  • methylenetetrahydrofolate dehydrogenase (NAD+) activity Source: UniProtKB
  • methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB
  • phosphate ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Magnesium, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Short name:
DNMDMC
Including the following 2 domains:
NAD-dependent methylenetetrahydrofolate dehydrogenase (EC:1.5.1.15)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Gene namesi
Name:Nmdmc
ORF Names:CG18466
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010222. Nmdmc.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 309Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrialPRO_0000034051
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiQ04448.

Expressioni

Developmental stagei

Expressed in developing tissues and at high levels in adult tissues. Isoform A shows male-specific expression.1 Publication

Gene expression databases

BgeeiQ04448.
GenevisibleiQ04448. DM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi71042. 1 interaction.
STRINGi7227.FBpp0081476.

Structurei

3D structure databases

ProteinModelPortaliQ04448.
SMRiQ04448. Positions 8-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0089. Eukaryota.
COG0190. LUCA.
GeneTreeiENSGT00840000129764.
InParanoidiQ04448.
KOiK13403.
OMAiGQPMALM.
OrthoDBiEOG7CG70C.
PhylomeDBiQ04448.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: Q04448-1) [UniParc]FASTAAdd to basket

Also known as: Hedengren-A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRFTSNMAQI IDGKAIAQEV RTQLAHELKG MEAAGYPKPH LTAVIVGEDP
60 70 80 90 100
ASEKYVANKM VACREVGISS ETKRLPASTT QEELLQLIAD LNKDPQVTGI
110 120 130 140 150
LVQLPVPEHI NERTICNAVD VDKDVDGFNE VNIGRTALDM EANIPATPLG
160 170 180 190 200
VKRLLEHMKI ETLGRNAVVV GRSKNVSLPM AILLHADGKY ATKAMDATVT
210 220 230 240 250
ICHRYTPPKE LARHCRQADI IVVAVGKPGL ITKDMVKPGA CVIDVGINRI
260 270 280 290 300
KDESTGQFKL VGDVDFEEVR QVAGHITPVP GGVGPMTVAM LMHNTLKAAR

KQFDDRKSS
Length:309
Mass (Da):33,551
Last modified:November 22, 2005 - v2
Checksum:i9E6846282570F457
GO
Isoform A (identifier: Q04448-2) [UniParc]FASTAAdd to basket

Also known as: Hedengren-B

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Show »
Length:303
Mass (Da):32,814
Checksum:iC925101D096B1358
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 44MRFT → MATVMGPTPPGTGVMWPAIW RTSSKAIGIRQSVQFEFSTR KISQKPQKEVTI (PubMed:8485162).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66Missing in isoform A. CuratedVSP_016458

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07958 mRNA. Translation: AAB41352.1.
AF186073 Genomic DNA. Translation: AAF07929.1.
AF186073 Genomic DNA. Translation: AAF07930.1.
AE014297 Genomic DNA. Translation: AAF54332.1.
AE014297 Genomic DNA. Translation: AAN13408.1.
AY047498 mRNA. Translation: AAK77230.1.
PIRiS32562.
RefSeqiNP_001262398.1. NM_001275469.1. [Q04448-2]
NP_476929.1. NM_057581.5. [Q04448-1]
NP_476930.1. NM_057582.5. [Q04448-2]
UniGeneiDm.33471.

Genome annotation databases

EnsemblMetazoaiFBtr0081996; FBpp0081476; FBgn0010222. [Q04448-1]
GeneIDi47895.
KEGGidme:Dmel_CG18466.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07958 mRNA. Translation: AAB41352.1.
AF186073 Genomic DNA. Translation: AAF07929.1.
AF186073 Genomic DNA. Translation: AAF07930.1.
AE014297 Genomic DNA. Translation: AAF54332.1.
AE014297 Genomic DNA. Translation: AAN13408.1.
AY047498 mRNA. Translation: AAK77230.1.
PIRiS32562.
RefSeqiNP_001262398.1. NM_001275469.1. [Q04448-2]
NP_476929.1. NM_057581.5. [Q04448-1]
NP_476930.1. NM_057582.5. [Q04448-2]
UniGeneiDm.33471.

3D structure databases

ProteinModelPortaliQ04448.
SMRiQ04448. Positions 8-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi71042. 1 interaction.
STRINGi7227.FBpp0081476.

Proteomic databases

PaxDbiQ04448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081996; FBpp0081476; FBgn0010222. [Q04448-1]
GeneIDi47895.
KEGGidme:Dmel_CG18466.

Organism-specific databases

CTDi47895.
FlyBaseiFBgn0010222. Nmdmc.

Phylogenomic databases

eggNOGiKOG0089. Eukaryota.
COG0190. LUCA.
GeneTreeiENSGT00840000129764.
InParanoidiQ04448.
KOiK13403.
OMAiGQPMALM.
OrthoDBiEOG7CG70C.
PhylomeDBiQ04448.

Miscellaneous databases

ChiTaRSiNmdmc. fly.
GenomeRNAii47895.
NextBioi839208.
PROiQ04448.

Gene expression databases

BgeeiQ04448.
GenevisibleiQ04448. DM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
    Price B.D., Laughon A.
    Biochim. Biophys. Acta 1173:94-98(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  2. "Relish, a central factor in the control of humoral, but not cellular immunity in Drosophila."
    Hedengren M., Asling B., Dushay M.S., Ando I., Ekengren S., Wihlborg M., Hultmark D.
    Mol. Cell 4:827-837(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiMTDC_DROME
AccessioniPrimary (citable) accession number: Q04448
Secondary accession number(s): Q7KSU1, Q9U6H6, Q9V3H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 22, 2005
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This NAD-dependent bifunctional enzyme has very different kinetic properties than the larger NADP-dependent trifunctional enzyme and is unique in that it requires formation of an enzyme-magnesium complex to allow binding of NAD.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.