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P80405

- MTHFS_RABIT

UniProt

P80405 - MTHFS_RABIT

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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene
MTHFS
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids By similarity.

Catalytic activityi

ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate.

Cofactori

Magnesium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611Substrate By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei189 – 1891ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 145ATP By similarity
Nucleotide bindingi147 – 1548ATP By similarity

GO - Molecular functioni

  1. 5-formyltetrahydrofolate cyclo-ligase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. folic acid binding Source: UniProtKB-KW

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. tetrahydrofolate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Folate-binding, Magnesium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
5-formyltetrahydrofolate cyclo-ligase (EC:6.3.3.2)
Alternative name(s):
5,10-methenyl-tetrahydrofolate synthetase
Short name:
MTHFS
Short name:
Methenyl-THF synthetase
Gene namesi
Name:MTHFS
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

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 – 2012015-formyltetrahydrofolate cyclo-ligasePRO_0000200277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000023444.

Structurei

3D structure databases

ProteinModelPortaliP80405.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1525Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG271145.
HOVERGENiHBG052525.

Family and domain databases

Gene3Di3.40.50.10420. 1 hit.
InterProiIPR002698. FTHF_cligase.
IPR024185. FTHF_cligase-like.
[Graphical view]
PANTHERiPTHR23407:SF1. PTHR23407:SF1. 1 hit.
PfamiPF01812. 5-FTHF_cyc-lig. 1 hit.
[Graphical view]
PIRSFiPIRSF006806. FTHF_cligase. 1 hit.
TIGRFAMsiTIGR02727. MTHFS_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P80405-1 [UniParc]FASTAAdd to Basket

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AAAAAVSGAK RSLRAELKQR LRAISAEERL RCQRLLTQKV IAHRQYQKSQ    50
RISIFLSMPD EIETEEIIKD IFQQGKVCFI PRYRLQSNHM DMVKLASADE 100
ISSLPKTSWN IHQPSESDTR EEALATGGLD LIFMPGLGFD RNGNRLGRGR 150
GYYDTYLQRC LQQQGAKPYT IALAFREQIC PQVPVDDTDV SVDEVLYVDA 200
A 201
Length:201
Mass (Da):22,733
Last modified:November 1, 1995 - v1
Checksum:i6FD20B8D9C31EC46
GO

Sequence databases

PIRiA53688.

Cross-referencesi

Sequence databases

PIRi A53688.

3D structure databases

ProteinModelPortali P80405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000023444.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG271145.
HOVERGENi HBG052525.

Family and domain databases

Gene3Di 3.40.50.10420. 1 hit.
InterProi IPR002698. FTHF_cligase.
IPR024185. FTHF_cligase-like.
[Graphical view ]
PANTHERi PTHR23407:SF1. PTHR23407:SF1. 1 hit.
Pfami PF01812. 5-FTHF_cyc-lig. 1 hit.
[Graphical view ]
PIRSFi PIRSF006806. FTHF_cligase. 1 hit.
TIGRFAMsi TIGR02727. MTHFS_bact. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase."
    Maras B., Stover P., Valiante S., Barra D., Schirch V.
    J. Biol. Chem. 269:18429-18433(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiMTHFS_RABIT
AccessioniPrimary (citable) accession number: P80405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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