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Q5R8P0

- C1TC_PONAB

UniProt

Q5R8P0 - C1TC_PONAB

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Protein
C-1-tetrahydrofolate synthase, cytoplasmic
Gene
MTHFD1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei197 – 1971NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1743NADP By similarity
Nucleotide bindingi380 – 3878ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: UniProtKB-EC
  3. methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB-EC
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB-EC

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. histidine biosynthetic process Source: UniProtKB-KW
  3. methionine biosynthetic process Source: UniProtKB-KW
  4. purine nucleotide biosynthetic process Source: UniProtKB-KW
  5. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Cleaved into the following chain:
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
Name:MTHFD1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935C-1-tetrahydrofolate synthase, cytoplasmicUniRule annotation
PRO_0000265955Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 935934C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processedUniRule annotation
PRO_0000423282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ5R8P0.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5R8P0.
SMRiQ5R8P0. Positions 2-296, 469-531.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305Methylenetetrahydrofolate dehydrogenase and cyclohydrolase By similarity
Add
BLAST
Regioni52 – 565Substrate binding By similarity
Regioni99 – 1013Substrate binding By similarity
Regioni272 – 2765Substrate binding By similarity
Regioni306 – 935630Formyltetrahydrofolate synthetaseUniRule annotation
Add
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG004916.
InParanoidiQ5R8P0.
KOiK00288.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. 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]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. 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]

Sequencei

Sequence statusi: Complete.

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

Q5R8P0-1 [UniParc]FASTAAdd to Basket

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MAPAEILNGR EISAQIRARL KNQVTQLKEQ VPGFTPGLAI LLVGNRDDSN    50
LYINVKLKAA EEIGIKATHI KLPRTTTESE VIKYITSLNE DSTVHGFLVQ 100
LPLDSENSIN TEEVINAIAP EKDVDGLTSI SAGKLARGDL NDCFIPCTPK 150
GCLELIKETG VPIAGRHAVV VGRSKIVGAP MHDLLLWNNA TVTTCHSKTA 200
NLDEEVNKGD ILVVATGRPE MVKGEWIKPG AIVIDCGINY VPDDKKPNGR 250
KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AKRFLEKFKP 300
GKWMIQYNNL NLKTPDPSDI DISRSCKPKP IGKLAREIGL LSEEVELYGE 350
TKAKVLLSAL ERLKHRPDGK YVVVTGITPT PLGEGKSTTT VGLVQALGAH 400
LYQNVFACVR QPSQGPTFGI KGGAAGGGYS QVIPMEEFNL HLTGDIHAFT 450
AANNLVAAAI DARIFHELTQ TDKALFNRLV PSVNGVRKFS DIQIRRLKRL 500
GIEKTDPTTL TDEEINRFAR LDIDPETITW QRVLDTNDRF LRKITIGQAP 550
TEKGHTRTAQ FDISVASEIM AALALTTSLE DMRERLGKMV VASSKKGEPV 600
SAEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII 650
ADRIALKLVG PEGFVVTEAG FGADIGMEKF FNIKCRYSGL CPHVVVLVAT 700
VRALKMHGGG PTVTAGLPLP KAYIEENLEL VEKGFSNLKK QIENARMFGI 750
PVVVAVNAFK TDTEAELDLI SRLSREHGAF DAVKCTHWAE GGNGALALAQ 800
AVQRAAQAPS SFQLLYDLKL PVEDKIRIIA QKIYGADDIE LLPEAQHKAE 850
VYTKQGFGNL PVCMAKTHLS LSHNPEQKGV PTGFILPIRD IRASVGAGFL 900
YPLVGTMSTM PGLPTRPCFY DIDLDPETQQ VNGLF 935
Length:935
Mass (Da):101,341
Last modified:January 23, 2007 - v3
Checksum:i4D98F58C5A908632
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859711 mRNA. Translation: CAH91870.1.
RefSeqiNP_001126083.1. NM_001132611.1.

Genome annotation databases

GeneIDi100173036.
KEGGipon:100173036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859711 mRNA. Translation: CAH91870.1 .
RefSeqi NP_001126083.1. NM_001132611.1.

3D structure databases

ProteinModelPortali Q5R8P0.
SMRi Q5R8P0. Positions 2-296, 469-531.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R8P0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173036.
KEGGi pon:100173036.

Organism-specific databases

CTDi 4522.

Phylogenomic databases

HOVERGENi HBG004916.
InParanoidi Q5R8P0.
KOi K00288.

Enzyme and pathway databases

UniPathwayi UPA00193 .

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. 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 ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. 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 ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiC1TC_PONAB
AccessioniPrimary (citable) accession number: Q5R8P0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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