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A2SKX8

- FTHS_METPP

UniProt

A2SKX8 - FTHS_METPP

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Protein

Formate--tetrahydrofolate ligase

Gene

fhs

Organism
Methylibium petroleiphilum (strain PM1)
Status
Reviewed - 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 bindingi66 – 738ATPUniRule 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

BioCyciMPET420662:GHBE-3302-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
Ordered Locus Names:Mpe_A3264
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
ProteomesiUP000000366: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Formate--tetrahydrofolate ligasePRO_0000293046Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi420662.Mpe_A3264.

Structurei

3D structure databases

ProteinModelPortaliA2SKX8.
SMRiA2SKX8. Positions 4-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2759.
HOGENOMiHOG000040280.
KOiK01938.
OMAiLKHHGGV.
OrthoDBiEOG6PCPSP.

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.

A2SKX8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASDIEIAQK ATLRRITQVA SDKLGIADEH LEPYGHYKAK LSLDYVDSLK
60 70 80 90 100
DRPNGKLILV TAISPTPAGE GKTTTTVGLG DALNRIGKKT LVCLREPSLG
110 120 130 140 150
PVFGMKGGAA GGGHAQVVPM EDINLHFTGD FNAIQLANNL LAAMIDNHIH
160 170 180 190 200
HGNELDIDVR RITWKRVLDM NDRALRDITC SLGGPGNGYP REDGFDIVVA
210 220 230 240 250
SEVMAIFCLA TSIQDLKERL GNIVVGYTRQ QKPVTARDLK AHGAMTVLLK
260 270 280 290 300
DALKPNLVQT LENNPAILHG GPFANIAHGC NSVIATQTSL KLADYVVTEA
310 320 330 340 350
GFGADLGAEK FIDIKCRKSG LRPDAVVLVA TIRALKFHGG VDVKELNTEN
360 370 380 390 400
LDALEKGIAN IERHVANIRE HYGLPCVVSI NNFTFDTPAE LKLLQDRMAK
410 420 430 440 450
HEVPVIVARH WAEGGKGAED VARAVVEIVE KGQSGAAGFK FVYDESLPLM
460 470 480 490 500
DKITAIATKI YGAAKVNASA KVAGEIKKLQ DAGYGHYPVC VAKTQYSFST
510 520 530 540 550
NPSARGAPSG HTIDIREVRL AAGAEFIVMI CGDVMTMPGL PKVPSAEKID
560
LGDDGKVVGL F
Length:561
Mass (Da):60,140
Last modified:March 6, 2007 - v1
Checksum:i8114C016F8B97EE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM96217.1.
RefSeqiWP_011830840.1. NC_008825.1.
YP_001022452.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM96217; ABM96217; Mpe_A3264.
GeneIDi4786483.
KEGGimpt:Mpe_A3264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM96217.1 .
RefSeqi WP_011830840.1. NC_008825.1.
YP_001022452.1. NC_008825.1.

3D structure databases

ProteinModelPortali A2SKX8.
SMRi A2SKX8. Positions 4-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420662.Mpe_A3264.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM96217 ; ABM96217 ; Mpe_A3264 .
GeneIDi 4786483.
KEGGi mpt:Mpe_A3264.

Phylogenomic databases

eggNOGi COG2759.
HOGENOMi HOG000040280.
KOi K01938.
OMAi LKHHGGV.
OrthoDBi EOG6PCPSP.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci MPET420662:GHBE-3302-MONOMER.

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. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiFTHS_METPP
AccessioniPrimary (citable) accession number: A2SKX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 6, 2007
Last modified: October 1, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3