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Protein

Formate--tetrahydrofolate ligase

Gene

fhs

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

Functioni

Catalytic activityi

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

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi68 – 75ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

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.
BRENDAi6.3.4.3. 1528.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001993611 – 559Formate--tetrahydrofolate ligaseAdd BLAST559

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi264732.Moth_0109.

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 24Combined sources6
Turni25 – 27Combined sources3
Helixi30 – 32Combined sources3
Beta strandi33 – 39Combined sources7
Beta strandi41 – 43Combined sources3
Helixi46 – 51Combined sources6
Beta strandi58 – 66Combined sources9
Helixi74 – 87Combined sources14
Beta strandi92 – 96Combined sources5
Helixi103 – 106Combined sources4
Beta strandi112 – 114Combined sources3
Beta strandi117 – 120Combined sources4
Helixi122 – 126Combined sources5
Turni127 – 130Combined sources4
Helixi132 – 152Combined sources21
Helixi161 – 163Combined sources3
Beta strandi168 – 172Combined sources5
Helixi175 – 177Combined sources3
Beta strandi178 – 183Combined sources6
Helixi187 – 189Combined sources3
Beta strandi193 – 195Combined sources3
Beta strandi197 – 199Combined sources3
Helixi200 – 202Combined sources3
Helixi204 – 211Combined sources8
Helixi215 – 223Combined sources9
Beta strandi226 – 230Combined sources5
Beta strandi235 – 237Combined sources3
Helixi239 – 241Combined sources3
Helixi244 – 250Combined sources7
Turni251 – 255Combined sources5
Beta strandi258 – 262Combined sources5
Beta strandi267 – 270Combined sources4
Beta strandi276 – 279Combined sources4
Helixi285 – 294Combined sources10
Beta strandi296 – 304Combined sources9
Turni306 – 308Combined sources3
Helixi309 – 315Combined sources7
Helixi317 – 321Combined sources5
Beta strandi327 – 332Combined sources6
Helixi334 – 339Combined sources6
Turni340 – 342Combined sources3
Helixi345 – 347Combined sources3
Helixi353 – 371Combined sources19
Turni372 – 374Combined sources3
Beta strandi377 – 382Combined sources6
Helixi389 – 398Combined sources10
Turni399 – 401Combined sources3
Beta strandi402 – 407Combined sources6
Turni412 – 414Combined sources3
Helixi415 – 419Combined sources5
Helixi420 – 432Combined sources13
Beta strandi443 – 445Combined sources3
Helixi447 – 457Combined sources11
Beta strandi462 – 466Combined sources5
Helixi468 – 479Combined sources12
Turni480 – 484Combined sources5
Beta strandi487 – 490Combined sources4
Beta strandi495 – 498Combined sources4
Beta strandi510 – 513Combined sources4
Beta strandi517 – 519Combined sources3
Turni520 – 522Combined sources3
Beta strandi523 – 527Combined sources5
Helixi543 – 545Combined sources3
Beta strandi551 – 555Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21164.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CKU. Bacteria.
COG2759. LUCA.

Family and domain databases

CDDicd00477. FTHFS. 1 hit.
Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01543. FTHFS. 1 hit.
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

        10         20         30         40         50
MSKVPSDIEI AQAAKMKPVM ELARGLGIQE DEVELYGKYK AKISLDVYRR
60 70 80 90 100
LKDKPDGKLI LVTAITPTPA GEGKTTTSVG LTDALARLGK RVMVCLREPS
110 120 130 140 150
LGPSFGIKGG AAGGGYAQVV PMEDINLHFT GDIHAVTYAH NLLAAMVDNH
160 170 180 190 200
LQQGNVLNID PRTITWRRVI DLNDRALRNI VIGLGGKANG VPRETGFDIS
210 220 230 240 250
VASEVMACLC LASDLMDLKE RFSRIVVGYT YDGKPVTAGD LEAQGSMALL
260 270 280 290 300
MKDAIKPNLV QTLENTPAFI HGGPFANIAH GCNSIIATKT ALKLADYVVT
310 320 330 340 350
EAGFGADLGA EKFYDVKCRY AGFKPDATVI VATVRALKMH GGVPKSDLAT
360 370 380 390 400
ENLEALREGF ANLEKHIENI GKFGVPAVVA INAFPTDTEA ELNLLYELCA
410 420 430 440 450
KAGAEVALSE VWAKGGEGGL ELARKVLQTL ESRPSNFHVL YNLDLSIKDK
460 470 480 490 500
IAKIATEIYG ADGVNYTAEA DKAIQRYESL GYGNLPVVMA KTQYSFSDDM
510 520 530 540 550
TKLGRPRNFT ITVREVRLSA GGRLIVPITG AIMTMPGLPK RPAACNIDID

ADGVITGLF
Length:559
Mass (Da):59,993
Last modified:May 1, 1991 - v1
Checksum:i36CD2BBB3C909B62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02911 Genomic DNA. Translation: AAA23240.1.
PIRiA35942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02911 Genomic DNA. Translation: AAA23240.1.
PIRiA35942.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264732.Moth_0109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CKU. Bacteria.
COG2759. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciMetaCyc:FORMYLSYNTHCLTH-MONOMER.
BRENDAi6.3.4.3. 1528.

Miscellaneous databases

EvolutionaryTraceiP21164.

Family and domain databases

CDDicd00477. FTHFS. 1 hit.
Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01543. FTHFS. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 88 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.