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Q5R8P0 (C1TC_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-1-tetrahydrofolate synthase, cytoplasmic

Short name=C1-THF synthase

Including the following 3 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
  3. Formyltetrahydrofolate synthetase
    EC=6.3.4.3
Gene names
Name:MTHFD1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length935 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01543

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01543

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01543.

Domain

This trifunctional enzyme consists of two major domains: a N-terminal part, containing the methylene-THF dehydrogenase and the methenyl-THF cyclohydrolase activities and a larger formyl-THF synthetase domain. HAMAP-Rule MF_01543

Sequence similarities

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 935935C-1-tetrahydrofolate synthase, cytoplasmic HAMAP-Rule MF_01543
PRO_0000265955
Initiator methionine11Removed; alternate By similarity
Chain2 – 935934C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed HAMAP-Rule MF_01543
PRO_0000423282

Regions

Nucleotide binding172 – 1743NADP By similarity
Nucleotide binding380 – 3878ATP By similarity
Region1 – 305305Methylenetetrahydrofolate dehydrogenase and cyclohydrolase By similarity
Region52 – 565Substrate binding By similarity
Region99 – 1013Substrate binding By similarity
Region272 – 2765Substrate binding By similarity
Region306 – 935630Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543

Sites

Binding site1971NADP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R8P0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4D98F58C5A908632

FASTA935101,341
        10         20         30         40         50         60 
MAPAEILNGR EISAQIRARL KNQVTQLKEQ VPGFTPGLAI LLVGNRDDSN LYINVKLKAA 

        70         80         90        100        110        120 
EEIGIKATHI KLPRTTTESE VIKYITSLNE DSTVHGFLVQ LPLDSENSIN TEEVINAIAP 

       130        140        150        160        170        180 
EKDVDGLTSI SAGKLARGDL NDCFIPCTPK GCLELIKETG VPIAGRHAVV VGRSKIVGAP 

       190        200        210        220        230        240 
MHDLLLWNNA TVTTCHSKTA NLDEEVNKGD ILVVATGRPE MVKGEWIKPG AIVIDCGINY 

       250        260        270        280        290        300 
VPDDKKPNGR KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AKRFLEKFKP 

       310        320        330        340        350        360 
GKWMIQYNNL NLKTPDPSDI DISRSCKPKP IGKLAREIGL LSEEVELYGE TKAKVLLSAL 

       370        380        390        400        410        420 
ERLKHRPDGK YVVVTGITPT PLGEGKSTTT VGLVQALGAH LYQNVFACVR QPSQGPTFGI 

       430        440        450        460        470        480 
KGGAAGGGYS QVIPMEEFNL HLTGDIHAFT AANNLVAAAI DARIFHELTQ TDKALFNRLV 

       490        500        510        520        530        540 
PSVNGVRKFS DIQIRRLKRL GIEKTDPTTL TDEEINRFAR LDIDPETITW QRVLDTNDRF 

       550        560        570        580        590        600 
LRKITIGQAP TEKGHTRTAQ FDISVASEIM AALALTTSLE DMRERLGKMV VASSKKGEPV 

       610        620        630        640        650        660 
SAEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII ADRIALKLVG 

       670        680        690        700        710        720 
PEGFVVTEAG FGADIGMEKF FNIKCRYSGL CPHVVVLVAT VRALKMHGGG PTVTAGLPLP 

       730        740        750        760        770        780 
KAYIEENLEL VEKGFSNLKK QIENARMFGI PVVVAVNAFK TDTEAELDLI SRLSREHGAF 

       790        800        810        820        830        840 
DAVKCTHWAE GGNGALALAQ AVQRAAQAPS SFQLLYDLKL PVEDKIRIIA QKIYGADDIE 

       850        860        870        880        890        900 
LLPEAQHKAE VYTKQGFGNL PVCMAKTHLS LSHNPEQKGV PTGFILPIRD IRASVGAGFL 

       910        920        930 
YPLVGTMSTM PGLPTRPCFY DIDLDPETQQ VNGLF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859711 mRNA. Translation: CAH91870.1.
RefSeqNP_001126083.1. NM_001132611.1.

3D structure databases

ProteinModelPortalQ5R8P0.
SMRQ5R8P0. Positions 2-296, 469-531.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R8P0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173036.
KEGGpon:100173036.

Organism-specific databases

CTD4522.

Phylogenomic databases

HOVERGENHBG004916.
InParanoidQ5R8P0.
KOK00288.

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1TC_PONAB
AccessionPrimary (citable) accession number: Q5R8P0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 61 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways