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P21164

- FTHS_MOOTH

UniProt

P21164 - FTHS_MOOTH

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Protein

Formate--tetrahydrofolate ligase

Gene
fhs
Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 758ATP By similarity

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
Complete GO annotation...

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 ligase (EC:6.3.4.3)
Alternative name(s):
Formyltetrahydrofolate synthetase
Short name:
FHS
Short name:
FTHFS
Gene namesi
Name:fhs
OrganismiMoorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifieri1525 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Formate--tetrahydrofolate ligaseUniRule annotationPRO_0000199361Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP21164.

Family & Domainsi

Sequence similaritiesi

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: April 16, 2014
This is version 77 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

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