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Database: UniProt
Entry: O66164
LinkDB: O66164
Original site: O66164 
ID   FTHS_SPHPI              Reviewed;         557 AA.
AC   O66164; Q60FW9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   19-FEB-2014, entry version 50.
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=ligH;
OS   Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=13689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SYK-6;
RX   PubMed=9501423;
RA   Nishikawa S., Sonoki T., Kasahara T., Obi T., Kubota S., Kawai S.,
RA   Morohoshi N., Katayama Y.;
RT   "Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis
RT   gene essential for the O demethylation of vanillate and syringate.";
RL   Appl. Environ. Microbiol. 64:836-842(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SYK-6;
RX   PubMed=15743951; DOI=10.1128/JB.187.6.2030-2037.2005;
RA   Abe T., Masai E., Miyauchi K., Katayama Y., Fukuda M.;
RT   "A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for
RT   catabolism of vanillate and syringate in Sphingomonas paucimobilis
RT   SYK-6.";
RL   J. Bacteriol. 187:2030-2037(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP +
CC       phosphate + 10-formyltetrahydrofolate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase
CC       family.
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DR   EMBL; AB006079; BAA25140.1; -; Genomic_DNA.
DR   EMBL; AB186750; BAD61061.1; -; Genomic_DNA.
DR   ProteinModelPortal; O66164; -.
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   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   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT   CHAIN         1    557       Formate--tetrahydrofolate ligase.
FT                                /FTId=PRO_0000199370.
FT   NP_BIND      67     74       ATP (By similarity).
FT   CONFLICT     13     14       ER -> AK (in Ref. 2; BAD61061).
FT   CONFLICT    175    175       V -> AL (in Ref. 2; BAD61061).
FT   CONFLICT    427    427       H -> L (in Ref. 2; BAD61061).
SQ   SEQUENCE   557 AA;  59423 MW;  D296E7538F6C8E86 CRC64;
     MAQGSDIEIA REERMQNIAE VGAKVGIPQD ALLNYGPYKA KLSWDFINSV QGNQDGKLIL
     VTAINPTPAG EGKTTTTVGL ADGLNRIGKK TVAALREPSL GPCFGVKGGA AGGGYAQVVP
     MEDINLHFTG DFHAITSANN LLAALIDNHI YWGNKLGLDP RRIAWRRVLD MNDRVRSIVN
     SLGGVSNGYP REDGFDITVA SEVMAILCLS SDLKDLERRL GNIHAGYTRE RKAVLASELN
     ASGAMTVLLK DALQPNMVQT LENNPVLIHG GPFANIAHGC NSVLATKTAL KIADYVVTEA
     GFGADLGAEK FFDIKCRKAG LKPSAAVIVA TIRALKMHGG VDKADLGTAN PEAVRKGGVN
     LARHIENVRQ FGVPVVVAIN QFITDTDEEM AMVKEIAEAA GAEAVLCSHW ANGSAGTEEL
     ARKVVAHAES GSSNFAPLYE DSMPLFEKID TIAKRIYRAT EATADSSVRN KLKGWEADGF
     GHLPVCMAKT QYSFSTDPAL RGAPTDHVVP VRDVILSAGA EFIVAVCGDI MRMPGLPKVP
     SADFIKLDEQ GQIQGLF
//
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