Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21164

- FTHS_MOOTH

UniProt

P21164 - FTHS_MOOTH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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 .
PIRi A35942.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 79 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