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Database: UniProt
Entry: Q83WS0
LinkDB: Q83WS0
Original site: Q83WS0 
ID   FTHS_METEA              Reviewed;         557 AA.
AC   Q83WS0; C5AS46;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   14-MAY-2014, entry version 56.
DE   RecName: Full=Formate--tetrahydrofolate ligase;
DE            EC=6.3.4.3;
DE   AltName: Full=Formyltetrahydrofolate synthetase;
DE            Short=FHS;
DE            Short=FTHFS;
GN   Name=fhs; Synonyms=ftfL; OrderedLocusNames=MexAM1_META1p0329;
OS   Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=14645277; DOI=10.1128/JB.185.24.7169-7175.2003;
RA   Marx C.J., Laukel M., Vorholt J.A., Lidstrom M.E.;
RT   "Purification of the formate-tetrahydrofolate ligase from
RT   Methylobacterium extorquens AM1 and demonstration of its requirement
RT   for methylotrophic growth.";
RL   J. Bacteriol. 185:7169-7175(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP +
CC       phosphate + 10-formyltetrahydrofolate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22 mM for formate;
CC         KM=0.8 mM for tetrahydrofolate;
CC         KM=21 uM for ATP;
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase
CC       family.
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DR   EMBL; AY279316; AAP33693.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS38281.1; -; Genomic_DNA.
DR   RefSeq; YP_002961558.1; NC_012808.1.
DR   ProteinModelPortal; Q83WS0; -.
DR   SMR; Q83WS0; 4-555.
DR   EnsemblBacteria; ACS38281; ACS38281; MexAM1_META1p0329.
DR   GeneID; 7990350; -.
DR   KEGG; mea:Mex_1p0329; -.
DR   PATRIC; 22506475; VBIMetExt101010_0354.
DR   eggNOG; COG2759; -.
DR   HOGENOM; HOG000040280; -.
DR   KO; K01938; -.
DR   OMA; LKHHGGV; -.
DR   OrthoDB; EOG6PCPSP; -.
DR   BioCyc; MetaCyc:MONOMER-3942; -.
DR   BioCyc; MEXT272630:GBY6-313-MONOMER; -.
DR   BRENDA; 6.3.4.3; 3296.
DR   SABIO-RK; Q83WS0; -.
DR   UniPathway; UPA00193; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01268; FTHFS; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Direct protein sequencing; Ligase;
KW   Nucleotide-binding; One-carbon metabolism.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    557       Formate--tetrahydrofolate ligase.
FT                                /FTId=PRO_0000199359.
FT   NP_BIND      65     72       ATP (By similarity).
SQ   SEQUENCE   557 AA;  59391 MW;  D0DB51A90971072A CRC64;
     MPSDIEIARA ATLKPIAQVA EKLGIPDEAL HNYGKHIAKI DHDFIASLEG KPEGKLVLVT
     AISPTPAGEG KTTTTVGLGD ALNRIGKRAV MCLREPSLGP CFGMKGGAAG GGKAQVVPME
     QINLHFTGDF HAITSAHSLA AALIDNHIYW ANELNIDVRR IHWRRVVDMN DRALRAINQS
     LGGVANGFPR EDGFDITVAS EVMAVFCLAK NLADLEERLG RIVIAETRDR KPVTLADVKA
     TGAMTVLLKD ALQPNLVQTL EGNPALIHGG PFANIAHGCN SVIATRTGLR LADYTVTEAG
     FGADLGAEKF IDIKCRQTGL KPSAVVIVAT IRALKMHGGV NKKDLQAENL DALEKGFANL
     ERHVNNVRSF GLPVVVGVNH FFQDTDAEHA RLKELCRDRL QVEAITCKHW AEGGAGAEAL
     AQAVVKLAEG EQKPLTFAYE TETKITDKIK AIATKLYGAA DIQIESKAAT KLAGFEKDGY
     GGLPVCMAKT QYSFSTDPTL MGAPSGHLVS VRDVRLSAGA GFVVVICGEI MTMPGLPKVP
     AADTIRLDAN GQIDGLF
//
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