ID   FTHS_VIBPA              Reviewed;         582 AA.
AC   Q87HX2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=VPA0834;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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}.
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DR   EMBL; BA000032; BAC62177.1; -; Genomic_DNA.
DR   RefSeq; NP_800344.1; NC_004605.1.
DR   RefSeq; WP_005479111.1; NC_004605.1.
DR   AlphaFoldDB; Q87HX2; -.
DR   SMR; Q87HX2; -.
DR   GeneID; 1191523; -.
DR   KEGG; vpa:VPA0834; -.
DR   PATRIC; fig|223926.6.peg.3764; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_6; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002493; Chromosome 2.
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;
KW   Reference proteome.
FT   CHAIN           1..582
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199409"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   582 AA;  62338 MW;  E8D2B79BE66F57D0 CRC64;
     MQSDIEICRN TPLSSIDVIA EKAGLLPEEF DTHGKYKAKV HPKCLARLND NQNGKLVLVT
     AITPTPLGEG KTVTTIGLAQ GLAKLKQSVM ACIRQPSMGP VFGIKGGAAG GGYSQVAPME
     ELNLHLTGDI HAVTAAHNLA SAALDARLFH EQREGYDAFE ARTGLKALKI DVESITWKRV
     MDHNDRALRM VKIGLNEHGK TINGFERNEG FDISAASELM AIIALAKNLK DLRQRIGKIV
     VAYDLDGQPI TTEDLQVAGA MAVTLKEAIA PTLMQTLEGV PTLIHAGPFA NIAHGNSSII
     ADEIALKLSR YTVTEAGFGS DMGFEKACNI KAAAANKAPD CVVIVATLRG LKANSGHYDL
     RPGMAIPDSI FSPDQAALVA GFENLKWHIK NVHKYGIPAV VAINQFPQDC EQELTALQDL
     IHAFDPNVKV AISTAFAQGG EGTRDLAQYV VDACEKTTNF RPLYQKHQSL QEKLMSVCEA
     GYGATNVEMS ELATKQLAHF EKLGFNELAV CIAKTPLSVT TDSSVKGAPV GFTVPIRELR
     LCAGAGFVYA LSGSVMTMPG LPDKPAFMNL DLDEDGNIIG LS
//