ID   FTHS_PARDP              Reviewed;         555 AA.
AC   A1B1M8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-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=fhs1 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=Pden_1317;
GN   and
GN   Name=fhs2 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=Pden_1580;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL69422.1; -; Genomic_DNA.
DR   EMBL; CP000489; ABL69680.1; -; Genomic_DNA.
DR   RefSeq; WP_011747640.1; NC_008686.1.
DR   AlphaFoldDB; A1B1M8; -.
DR   SMR; A1B1M8; -.
DR   STRING; 318586.Pden_1317; -.
DR   PRIDE; A1B1M8; -.
DR   EnsemblBacteria; ABL69422; ABL69422; Pden_1317.
DR   EnsemblBacteria; ABL69680; ABL69680; Pden_1580.
DR   KEGG; pde:Pden_1317; -.
DR   KEGG; pde:Pden_1580; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000361; Chromosome 1.
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_0000293050"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  58648 MW;  F998D8F43C47015E CRC64;
     MKSDIQIARE AQKLPIAQIA GRLGLAEADF LPYGHDKAKI AHEAIAALAG RPQGRLILVT
     AINPTPAGEG KTTTTVGLGD ALNRIGKRAT VCIREASLGP NFGMKGGAAG GGHAQIVPME
     DMNLHFTGDF HAVTSAHNLL AAMIDNHIHW GNALRIDPRR VTWRRVMDMN DRVLRQVVVA
     LGGPANGVPR ECGFDITVAS EVMAILCLAS DLADLQARLG RIVIGQTFDR RPVTAHDLGA
     EGAMTVLLRD ALQPNLVQTL ENNPALVHGG PFANIAHGCN SVMATRTALA LSDYVVTEAG
     FGADLGAEKF LNIKCRLAGL QPAAAVLVAT VRALKMNGGV ARTDLGAENV AALRAGCANL
     GRHIQNLRRF GLPVVVAINH FSGDTEAEIA ALADYCRERG VQAVLCRHWA EGGKGAEDLA
     RAVVALAEGG ADFTPLYPDE MPLAEKIETI CHRIYGAGQV EFLPHIVERL EEWQAAGHGH
     LPVCMAKTQY SFSANPAALG APEGFTIPVR EVRLAAGAGF VVAICGDIMT MPGLPREPSA
     LRIGVDADGH VQGLF