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Q0VCR7 (C1TM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Monofunctional C1-tetrahydrofolate synthase, mitochondrial

EC=6.3.4.3
Alternative name(s):
Formyltetrahydrofolate synthetase
Gene names
Name:MTHFD1L
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01543

Catalytic activity

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

Mitochondrion By similarity HAMAP-Rule MF_01543.

Domain

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. 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

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 975945Monofunctional C1-tetrahydrofolate synthase, mitochondrial HAMAP-Rule MF_01543
PRO_0000343176

Regions

Nucleotide binding420 – 4278ATP By similarity
Region31 – 345315Methylenetetrahydrofolate dehydrogenase and cyclohydrolase HAMAP-Rule MF_01543
Region346 – 975630Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543
Compositional bias33 – 419Poly-Gly HAMAP-Rule MF_01543

Amino acid modifications

Modified residue1871N6-acetyllysine; alternate By similarity
Modified residue1871N6-succinyllysine; alternate By similarity
Modified residue5931N6-succinyllysine By similarity

Experimental info

Sequence conflict1951E → G in AAI20039. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q0VCR7 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 4B7D0B35164A580B

FASTA975105,227
        10         20         30         40         50         60 
MSARLPFVLR RLARPQHPGS PRRLPSLCRA SSGRGSGCGG GEGLLGQQRL RDTQAGSSRG 

        70         80         90        100        110        120 
PGSPAPPARD SIVREVIQNS KEVLSLLQEK TPTFKPVLAI IQAGDDNLMQ EVNQNLAEEA 

       130        140        150        160        170        180 
GLNITHICLP AESGEDEIID EILKINEDSR VHGLALQIAE TSFSNKILNA LKPEKDVDGL 

       190        200        210        220        230        240 
TDVNLGKLVR GDAHECFISP VARAVIELLE KSGVSLDGKK ILVIGAHGSL EATLQCLFQR 

       250        260        270        280        290        300 
KGSMTMSSQW KTPQLQGKLQ EADIVVLGSP KPEEIPLSWI QPGTTVFNCS HDFLSGKAAC 

       310        320        330        340        350        360 
ISSGVHGISP IAEDVSLLAA ALRIQNMVSS GRRWLREQQH RRWRLHCLKL QPLSPVPSDI 

       370        380        390        400        410        420 
EISRAQTPKA VEILAKEIGL LADEIEIYGK SKAKVRLSLL ERLKDQADGK YVLVAGITPT 

       430        440        450        460        470        480 
PLGEGKSTVT IGLVQALTAH LNVNSFACLR QPSQGPTFGV KGGAAGGGYA QVIPMEEFNL 

       490        500        510        520        530        540 
HLTGDIHAIT AANNLLAAAI DARILHENTQ TDKALYNRLV PSVNGVREFS KIQLARLKRL 

       550        560        570        580        590        600 
GINKTDPSAL TEEEMRKFAR LDIDPSTITW QRVVDTNDRF LRKITIGQAN TEKGCSRQAQ 

       610        620        630        640        650        660 
FDIAVASEIM AVLALTDSLS DMKERLGRMV VASDRNGQPV TADDLGVTGA LTVLMKDAIK 

       670        680        690        700        710        720 
PNLMQTLEGT PVFVHAGPFA NIAHGNSSVL ADKIALKLVG EGGFVVTEAG FGADIGMEKF 

       730        740        750        760        770        780 
FNIKCRASGL VPSVVVLVAT VRALKMHGGG PSVTAGVPLR KEYTEENLQL VADGCCNLEK 

       790        800        810        820        830        840 
QIQIAQLFGV PVVVALNVFK TDTRAEIDLV CELAKRAGAF NAVPCYHWSI GGKGSVDLAW 

       850        860        870        880        890        900 
AVREAASKES RFQFLYDVQL PIVEKIRTIA QSVYGAKDIE LSPEAQSKID RYTEQGFGNL 

       910        920        930        940        950        960 
PICMAKTHLS LSHQPDKKGV PKGFILPISD VRASIGAGFI YPLVGTMSTM PGLPTRPCFY 

       970 
DIDLDTETEQ VKGLF 

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver and Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120038 mRNA. Translation: AAI20039.1.
BC148878 mRNA. Translation: AAI48879.1.
RefSeqNP_001069486.1. NM_001076018.2.
UniGeneBt.7490.

3D structure databases

ProteinModelPortalQ0VCR7.
SMRQ0VCR7. Positions 509-571.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ0VCR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID534296.
KEGGbta:534296.

Organism-specific databases

CTD25902.

Phylogenomic databases

eggNOGCOG0190.
HOGENOMHOG000040280.
HOVERGENHBG004916.
InParanoidQ0VCR7.
KOK13402.

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 2 hits.
HAMAPMF_01543. FTHFS.
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.
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.
[Graphical view]
ProtoNetSearch...

Other

NextBio20876344.

Entry information

Entry nameC1TM_BOVIN
AccessionPrimary (citable) accession number: Q0VCR7
Secondary accession number(s): A6QNK9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 64 of the entry and version 2 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