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P21164

- FTHS_MOOTH

UniProt

P21164 - FTHS_MOOTH

Protein

Formate--tetrahydrofolate ligase

Gene

fhs

Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 758ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. formate-tetrahydrofolate ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. folic acid-containing compound biosynthetic process Source: InterPro
    2. tetrahydrofolate interconversion Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:FORMYLSYNTHCLTH-MONOMER.
    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate--tetrahydrofolate ligaseUniRule annotation (EC:6.3.4.3UniRule annotation)
    Alternative name(s):
    Formyltetrahydrofolate synthetaseUniRule annotation
    Short name:
    FHSUniRule annotation
    Short name:
    FTHFSUniRule annotation
    Gene namesi
    Name:fhsUniRule annotation
    OrganismiMoorella thermoacetica (Clostridium thermoaceticum)
    Taxonomic identifieri1525 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Formate--tetrahydrofolate ligasePRO_0000199361Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 246
    Turni25 – 273
    Helixi30 – 323
    Beta strandi33 – 397
    Beta strandi41 – 433
    Helixi46 – 516
    Beta strandi58 – 669
    Helixi74 – 8714
    Beta strandi92 – 965
    Helixi103 – 1064
    Beta strandi112 – 1143
    Beta strandi117 – 1204
    Helixi122 – 1265
    Turni127 – 1304
    Helixi132 – 15221
    Helixi161 – 1633
    Beta strandi168 – 1725
    Helixi175 – 1773
    Beta strandi178 – 1836
    Helixi187 – 1893
    Beta strandi193 – 1953
    Beta strandi197 – 1993
    Helixi200 – 2023
    Helixi204 – 2118
    Helixi215 – 2239
    Beta strandi226 – 2305
    Beta strandi235 – 2373
    Helixi239 – 2413
    Helixi244 – 2507
    Turni251 – 2555
    Beta strandi258 – 2625
    Beta strandi267 – 2704
    Beta strandi276 – 2794
    Helixi285 – 29410
    Beta strandi296 – 3049
    Turni306 – 3083
    Helixi309 – 3157
    Helixi317 – 3215
    Beta strandi327 – 3326
    Helixi334 – 3396
    Turni340 – 3423
    Helixi345 – 3473
    Helixi353 – 37119
    Turni372 – 3743
    Beta strandi377 – 3826
    Helixi389 – 39810
    Turni399 – 4013
    Beta strandi402 – 4076
    Turni412 – 4143
    Helixi415 – 4195
    Helixi420 – 43213
    Beta strandi443 – 4453
    Helixi447 – 45711
    Beta strandi462 – 4665
    Helixi468 – 47912
    Turni480 – 4845
    Beta strandi487 – 4904
    Beta strandi495 – 4984
    Beta strandi510 – 5134
    Beta strandi517 – 5193
    Turni520 – 5223
    Beta strandi523 – 5275
    Helixi543 – 5453
    Beta strandi551 – 5555

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG7X-ray2.50A/B1-559[»]
    1FP7X-ray3.20A/B1-559[»]
    1FPMX-ray3.00A/B1-559[»]
    3QUSX-ray2.84A/B1-559[»]
    4JIMX-ray2.20A/B1-559[»]
    4JJKX-ray3.00A/B1-559[»]
    4JJZX-ray2.50A/B1-559[»]
    4JKIX-ray2.67A/B1-559[»]
    ProteinModelPortaliP21164.
    SMRiP21164. Positions 7-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21164.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the formate--tetrahydrofolate ligase family.UniRule annotation

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_01543. FTHFS.
    InterProiIPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF01268. FTHFS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21164-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKVPSDIEI AQAAKMKPVM ELARGLGIQE DEVELYGKYK AKISLDVYRR    50
    LKDKPDGKLI LVTAITPTPA GEGKTTTSVG LTDALARLGK RVMVCLREPS 100
    LGPSFGIKGG AAGGGYAQVV PMEDINLHFT GDIHAVTYAH NLLAAMVDNH 150
    LQQGNVLNID PRTITWRRVI DLNDRALRNI VIGLGGKANG VPRETGFDIS 200
    VASEVMACLC LASDLMDLKE RFSRIVVGYT YDGKPVTAGD LEAQGSMALL 250
    MKDAIKPNLV QTLENTPAFI HGGPFANIAH GCNSIIATKT ALKLADYVVT 300
    EAGFGADLGA EKFYDVKCRY AGFKPDATVI VATVRALKMH GGVPKSDLAT 350
    ENLEALREGF ANLEKHIENI GKFGVPAVVA INAFPTDTEA ELNLLYELCA 400
    KAGAEVALSE VWAKGGEGGL ELARKVLQTL ESRPSNFHVL YNLDLSIKDK 450
    IAKIATEIYG ADGVNYTAEA DKAIQRYESL GYGNLPVVMA KTQYSFSDDM 500
    TKLGRPRNFT ITVREVRLSA GGRLIVPITG AIMTMPGLPK RPAACNIDID 550
    ADGVITGLF 559
    Length:559
    Mass (Da):59,993
    Last modified:May 1, 1991 - v1
    Checksum:i36CD2BBB3C909B62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02911 Genomic DNA. Translation: AAA23240.1.
    PIRiA35942.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02911 Genomic DNA. Translation: AAA23240.1 .
    PIRi A35942.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG7 X-ray 2.50 A/B 1-559 [» ]
    1FP7 X-ray 3.20 A/B 1-559 [» ]
    1FPM X-ray 3.00 A/B 1-559 [» ]
    3QUS X-ray 2.84 A/B 1-559 [» ]
    4JIM X-ray 2.20 A/B 1-559 [» ]
    4JJK X-ray 3.00 A/B 1-559 [» ]
    4JJZ X-ray 2.50 A/B 1-559 [» ]
    4JKI X-ray 2.67 A/B 1-559 [» ]
    ProteinModelPortali P21164.
    SMRi P21164. Positions 7-557.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    BioCyci MetaCyc:FORMYLSYNTHCLTH-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P21164.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_01543. FTHFS.
    InterProi IPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF01268. FTHFS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum."
      Lovell C.R., Przybyla A., Ljungdahl L.G.
      Biochemistry 29:5687-5694(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica."
      Radfar R., Shin R., Sheldrick G.M., Minor W., Lovell C.R., Odom J.D., Dunlap R.B., Lebioda L.
      Biochemistry 39:3920-3926(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
    3. "Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica."
      Radfar R., Leaphart A., Brewer J.M., Minor W., Odom J.D., Dunlap R.B., Lovell C.R., Lebioda L.
      Biochemistry 39:14481-14486(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MONOVALENT CATIONS.

    Entry informationi

    Entry nameiFTHS_MOOTH
    AccessioniPrimary (citable) accession number: P21164
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binding of monovalent cations contributes to thermal stability.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3