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