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Protein

Monofunctional C1-tetrahydrofolate synthase, mitochondrial

Gene

Mthfd1l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2.1 Publication

Catalytic activityi

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi422 – 429ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

  • 10-formyltetrahydrofolate biosynthetic process Source: MGI
  • embryonic neurocranium morphogenesis Source: BHF-UCL
  • embryonic viscerocranium morphogenesis Source: BHF-UCL
  • folic acid-containing compound metabolic process Source: MGI
  • formate metabolic process Source: MGI
  • neural tube closure Source: BHF-UCL
  • purine nucleobase biosynthetic process Source: GO_Central
  • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
  • tetrahydrofolate metabolic process Source: MGI

Keywordsi

Molecular functionLigase
Biological processOne-carbon metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.4.3 3474
ReactomeiR-MMU-196757 Metabolism of folate and pterines
UniPathwayiUPA00193

Names & Taxonomyi

Protein namesi
Recommended name:
Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC:6.3.4.3)
Alternative name(s):
Formyltetrahydrofolate synthetase
Gene namesi
Name:Mthfd1l
Synonyms:Fthfsdc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1924836 Mthfd1l

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 31MitochondrionSequence analysisAdd BLAST31
ChainiPRO_000034317832 – 977Monofunctional C1-tetrahydrofolate synthase, mitochondrialAdd BLAST946

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateCombined sources1
Modified residuei356PhosphoserineBy similarity1
Modified residuei595N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3V3R1
MaxQBiQ3V3R1
PaxDbiQ3V3R1
PeptideAtlasiQ3V3R1
PRIDEiQ3V3R1

2D gel databases

REPRODUCTION-2DPAGEiQ3V3R1

PTM databases

iPTMnetiQ3V3R1
PhosphoSitePlusiQ3V3R1
SwissPalmiQ3V3R1

Expressioni

Gene expression databases

BgeeiENSMUSG00000040675
GenevisibleiQ3V3R1 MM

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234813, 3 interactors
IntActiQ3V3R1, 9 interactors
MINTiQ3V3R1
STRINGi10090.ENSMUSP00000036178

Structurei

Secondary structure

1977
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi514 – 521Combined sources8
Beta strandi525 – 528Combined sources4
Helixi533 – 542Combined sources10
Turni549 – 551Combined sources3
Helixi554 – 562Combined sources9

3D structure databases

ProteinModelPortaliQ3V3R1
SMRiQ3V3R1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3V3R1

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 347Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd BLAST316
Regioni348 – 977Formyltetrahydrofolate synthetaseAdd BLAST630

Domaini

This monofunctional enzyme consists of two major domains: an N-terminal inactive methylene-THF dehydrogenase and cyclohydrolase domain and an active larger formyl-THF synthetase C-terminal domain.

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4230 Eukaryota
COG0190 LUCA
COG2759 LUCA
GeneTreeiENSGT00920000149058
HOGENOMiHOG000040280
HOVERGENiHBG004916
InParanoidiQ3V3R1
KOiK13402
OMAiCSHDFLS
OrthoDBiEOG091G01BU
PhylomeDBiQ3V3R1
TreeFamiTF300623

Family and domain databases

CDDicd00477 FTHFS, 1 hit
HAMAPiMF_01543 FTHFS, 1 hit
InterProiView protein in InterPro
IPR000559 Formate_THF_ligase
IPR020628 Formate_THF_ligase_CS
IPR036291 NAD(P)-bd_dom_sf
IPR027417 P-loop_NTPase
IPR000672 THF_DH/CycHdrlase
IPR020630 THF_DH/CycHdrlase_cat_dom
IPR020631 THF_DH/CycHdrlase_NAD-bd_dom
PfamiView protein in Pfam
PF01268 FTHFS, 1 hit
PF00763 THF_DHG_CYH, 1 hit
PF02882 THF_DHG_CYH_C, 1 hit
PRINTSiPR00085 THFDHDRGNASE
SUPFAMiSSF51735 SSF51735, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00721 FTHFS_1, 1 hit
PS00722 FTHFS_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q3V3R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRLPLLLR QLGRQQLPSG PACRLRELCR SGSRSSSSGG GDPEGLRGRR
60 70 80 90 100
LQDGQTFSSH GPGNPEAPGM DSIVRDVIHN SKEVLSLLQE KNPAFKPVLV
110 120 130 140 150
VIQAGDDNLM KDMNQNLAKE AGLDITHICL PPDSGEDEII DEILKINEDP
160 170 180 190 200
RVHGLTLQIS EDSLSNKVLN ALKPEKDVDG VTDINLGKLV RGDAPECFVS
210 220 230 240 250
PLAKAAVELV EKSGITLDGK KVLVVGAHGP LEAALQWLFQ RKGSMTMSCP
260 270 280 290 300
WATPQLPDKL READIVVLGS PKPEEIPAVW IPSGTTILNC FHDFLSGKLS
310 320 330 340 350
GGSPGVPVDK LIAEESVSLL AAALRIQNMV SSGRRWLREQ QHRRWRLHCL
360 370 380 390 400
KLQPLSPVPS DIEISRGQTP KAVDVLAKEI GLLADEIEIY GKSKAKVQLS
410 420 430 440 450
LLERLKDQTD GKYVLVAGIT PTPLGEGKST VTIGLVQALT AHLKVNSFAC
460 470 480 490 500
LRQPSQGPTF GVKGGAAGGG YAQVIPMEEF NLHLTGDIHA ITAANNLLAA
510 520 530 540 550
AIDTRILHES TQTDKALYNR LVPLVNGVRE FSEIQLSRLK KLGIHKTDPS
560 570 580 590 600
TLTEEEVRKF ARLNIDPATI TWQRVLDTND RFLRKITIGQ GSTEKGYSRQ
610 620 630 640 650
AQFDIAVASE IMAVLALTDS LTDMKERLGR MVVASDKDGQ PVTAEDLGVT
660 670 680 690 700
GALTVLMKDA IKPNLMQTLE GTPVFVHAGP FANIAHGNSS VLADKIALKL
710 720 730 740 750
VGEEGFVVTE AGFGADIGME KFFNIKCRAS GLVPNVVVLV ATVRALKMHG
760 770 780 790 800
GGPSVTAGVP LKKEYTEENI QLVADGCCNL QKQIQIAQLF GVPVVVALNV
810 820 830 840 850
FKTDTRAEID LVCELAKRAG AFDAVPCYHW SAGGKGSVDL ARAVREAANK
860 870 880 890 900
RSRFQFLYDV QLPIVEKIRV IAQTVYGAKD IELSPEAQSK IDRYTQQGFG
910 920 930 940 950
NLPICMAKTH LSLSHEPDKK GVPRDFTLPI SDVRASIGAG FIYPLVGTMS
960 970
TMPGLPTRPC FYDIDLDTET EQVKGLF
Length:977
Mass (Da):105,729
Last modified:July 1, 2008 - v2
Checksum:i7275EF6F9A4292D6
GO

Sequence cautioni

The sequence AAH30437 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti137D → N in BAE35568 (PubMed:16141072).Curated1
Sequence conflicti279V → A in BAE35568 (PubMed:16141072).Curated1
Sequence conflicti279V → A in AAH30437 (PubMed:15489334).Curated1
Sequence conflicti279V → A in AAH49936 (PubMed:15489334).Curated1
Sequence conflicti353Q → H in BAE35568 (PubMed:16141072).Curated1
Sequence conflicti369T → N in BAE20500 (PubMed:16141072).Curated1
Sequence conflicti419I → V in BAC30053 (PubMed:16141072).Curated1
Sequence conflicti422T → S in BAE35568 (PubMed:16141072).Curated1
Sequence conflicti632V → A in BAE35568 (PubMed:16141072).Curated1
Sequence conflicti963D → G in BAE20438 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038579 mRNA Translation: BAC30053.1
AK028211 mRNA Translation: BAE20438.1
AK036284 mRNA Translation: BAE20500.1
AK160025 mRNA Translation: BAE35568.1
BC030437 mRNA Translation: AAH30437.1 Different initiation.
BC049936 mRNA Translation: AAH49936.1
CCDSiCCDS56672.1
RefSeqiNP_001164256.1, NM_001170785.1
NP_001164257.1, NM_001170786.1
NP_758512.3, NM_172308.4
UniGeneiMm.184752

Genome annotation databases

EnsembliENSMUST00000043735; ENSMUSP00000036178; ENSMUSG00000040675
ENSMUST00000117291; ENSMUSP00000112870; ENSMUSG00000040675
ENSMUST00000120585; ENSMUSP00000112897; ENSMUSG00000040675
GeneIDi270685
KEGGimmu:270685
UCSCiuc007ehj.2 mouse

Similar proteinsi

Entry informationi

Entry nameiC1TM_MOUSE
AccessioniPrimary (citable) accession number: Q3V3R1
Secondary accession number(s): Q3TVQ0
, Q3V402, Q80V98, Q8CAL0, Q8K2N5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: June 20, 2018
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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