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Protein

Formate--tetrahydrofolate ligase

Gene

fhs

Organism
Sphingomonas paucimobilis (Pseudomonas paucimobilis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748ATPUniRule 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

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
Synonyms:ligH
OrganismiSphingomonas paucimobilis (Pseudomonas paucimobilis)
Taxonomic identifieri13689 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557Formate--tetrahydrofolate ligasePRO_0000199370Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO66164.
ModBaseiSearch...
MobiDBiSearch...

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.

O66164-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQGSDIEIA REERMQNIAE VGAKVGIPQD ALLNYGPYKA KLSWDFINSV
60 70 80 90 100
QGNQDGKLIL VTAINPTPAG EGKTTTTVGL ADGLNRIGKK TVAALREPSL
110 120 130 140 150
GPCFGVKGGA AGGGYAQVVP MEDINLHFTG DFHAITSANN LLAALIDNHI
160 170 180 190 200
YWGNKLGLDP RRIAWRRVLD MNDRVRSIVN SLGGVSNGYP REDGFDITVA
210 220 230 240 250
SEVMAILCLS SDLKDLERRL GNIHAGYTRE RKAVLASELN ASGAMTVLLK
260 270 280 290 300
DALQPNMVQT LENNPVLIHG GPFANIAHGC NSVLATKTAL KIADYVVTEA
310 320 330 340 350
GFGADLGAEK FFDIKCRKAG LKPSAAVIVA TIRALKMHGG VDKADLGTAN
360 370 380 390 400
PEAVRKGGVN LARHIENVRQ FGVPVVVAIN QFITDTDEEM AMVKEIAEAA
410 420 430 440 450
GAEAVLCSHW ANGSAGTEEL ARKVVAHAES GSSNFAPLYE DSMPLFEKID
460 470 480 490 500
TIAKRIYRAT EATADSSVRN KLKGWEADGF GHLPVCMAKT QYSFSTDPAL
510 520 530 540 550
RGAPTDHVVP VRDVILSAGA EFIVAVCGDI MRMPGLPKVP SADFIKLDEQ

GQIQGLF
Length:557
Mass (Da):59,423
Last modified:August 1, 1998 - v1
Checksum:iD296E7538F6C8E86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142ER → AK in BAD61061. (PubMed:15743951)Curated
Sequence conflicti175 – 1751V → AL in BAD61061. (PubMed:15743951)Curated
Sequence conflicti427 – 4271H → L in BAD61061. (PubMed:15743951)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006079 Genomic DNA. Translation: BAA25140.1.
AB186750 Genomic DNA. Translation: BAD61061.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006079 Genomic DNA. Translation: BAA25140.1.
AB186750 Genomic DNA. Translation: BAD61061.1.

3D structure databases

ProteinModelPortaliO66164.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00193.

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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate."
    Nishikawa S., Sonoki T., Kasahara T., Obi T., Kubota S., Kawai S., Morohoshi N., Katayama Y.
    Appl. Environ. Microbiol. 64:836-842(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SYK-6.
  2. "A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6."
    Abe T., Masai E., Miyauchi K., Katayama Y., Fukuda M.
    J. Bacteriol. 187:2030-2037(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SYK-6.

Entry informationi

Entry nameiFTHS_SPHPI
AccessioniPrimary (citable) accession number: O66164
Secondary accession number(s): Q60FW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 1, 1998
Last modified: October 1, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.