ID   FTHS_CUTAK              Reviewed;         563 AA.
AC   Q6ABS5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 118.
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=PPA0049;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT81808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017283; AAT81808.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6ABS5; -.
DR   SMR; Q6ABS5; -.
DR   EnsemblBacteria; AAT81808; AAT81808; PPA0049.
DR   KEGG; pac:PPA0049; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_11; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000603; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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..563
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199369"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   563 AA;  59660 MW;  6BE2573EA8575BA1 CRC64;
     MKSDLEIARE AHLDPIEKVA ARAGIDEKYL EPYGRGVAKV DLDVVTHNRD HSCGKYVVVT
     AMTPTPLGEG KTTTAVGLAQ GLEKIGKHSV LALRQPSMGP TFGIKGGAAG AGYSQVLPME
     KLNLHLTGDF HAIGAAHNLL AAMIDNHLHQ GNELDIEPHS ISWRRVVDIN DRALRNTIVG
     LGSRVDGVPR ETGFDITAAS EVGVILSLAT SLSDLRARLG RIVIGYNRSK EPVSAEDLHA
     AGSMAVILKD ALKPNLLQTT ENSPVLVHAG PFGNIATGNS SVIADRVGIG CGDYLLTEAG
     FGADMGAERF FNIKCRIGGM RPDAAVLVAT VRALKTHAGR YKVIPGKPLP PAMLEDNPDD
     VLAGAANLRK HIEIVREFGV SPIVALNVFP TDHPDEIDAV RKVAEAAGAH FASSTHVVDG
     GDGAVDLAHA VVAACDHKAD FRYTYDLEDS LVEKLTKVAT KVYGADGIDI APAAAKELAH
     FEDLGYGTFP VVIAKTHLSL SHDPSLKGAP TGWRLPVREV RAAVGAGYIY AICGDMRTMP
     GLGRHPAAER IDIDDNGETI GLF
//