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FTHS_PARD8
ID   FTHS_PARD8              Reviewed;         555 AA.
AC   A6LAR6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=BDI_1014;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC         formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR   EMBL; CP000140; ABR42780.1; -; Genomic_DNA.
DR   RefSeq; WP_005857104.1; NZ_LR215978.1.
DR   AlphaFoldDB; A6LAR6; -.
DR   SMR; A6LAR6; -.
DR   STRING; 435591.BDI_1014; -.
DR   EnsemblBacteria; ABR42780; ABR42780; BDI_1014.
DR   KEGG; pdi:BDI_1014; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_10; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   BioCyc; PDIS435591:G1G5A-1047-MON; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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;
KW   Reference proteome.
FT   CHAIN           1..555
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000300533"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  60156 MW;  F8AEF9F9C702CF8D CRC64;
     MKSDIEIARE TDLRKIKEVA TTLGIPREEV QNYGRYIAKV PIHLIDKKQM DQHNLILVTA
     ITPTKAGIGK TTVSIGLALG LNKIGKKAVV ALREPSLGPC FGMKGGAAGG GYAQVLPMEN
     INLHFTGDFH AVTSAHNMIT ALLDNYIYQT RNTCEGLKEI KWKRVLDVND RSLRNIVSGL
     GGSANGVPTE TGFDITPASE IMAILCLATD IEDLKRRVGN ILLGYTNEDK PFTVNDLGIA
     GAITVLLKDA LLPNLVQTTE NTPAFVHGGP FANIAHGCNS ISATQMALTY GDYVITEAGF
     GADLGAEKFF NIKCRKAGLS PKLTVIVATA QSLKLHGGVP EKEIKEPNIE GLKNGFANLD
     KHIENMKSFG QQVIVTFNRF ATDTDEEIAL VAEHCEEKGV GFAMNNVFAE GGEGGTELAR
     LVVDTIENHP SAPLQYTYDL NDPIRTKVQK VAQKIYGASS IVYTTLADKK LRQIESLGIS
     HYPICIAKTQ YSFSSDPKAY GVAKDFELKV RDVIINNGAE MIVVVMGEIM RMPGLPKEPQ
     ARKIDIVDGM IEGLS
 
 
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