FTHS_PHOPR
ID FTHS_PHOPR Reviewed; 584 AA.
AC Q6LNJ0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=PBPRA2764;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378672; CAG21136.1; -; Genomic_DNA.
DR RefSeq; WP_011219410.1; NC_006370.1.
DR AlphaFoldDB; Q6LNJ0; -.
DR SMR; Q6LNJ0; -.
DR STRING; 298386.PBPRA2764; -.
DR EnsemblBacteria; CAG21136; CAG21136; PBPRA2764.
DR KEGG; ppr:PBPRA2764; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000593; 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 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..584
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199367"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 584 AA; 61957 MW; C1887713A5A6490A CRC64;
MKSDIQICRD TALTPIDQIA LMAGIEPQDL TPQGTLKAKV KPSILNRLAD KPEGKLVLVT
AITPTPLGEG KTVTTIGLAQ GLAKINKRVI ACIRQPSMGP VFGVKGGAAG GGYSQVAPME
KLNLHLTGDI HAVTAAHNLA AAALDARLYH EERHGYEAFS DKTGLPALRI DIKNIVWKRV
MDHNDRALRM ITVGKNEAGK AINGLEREDG FDISAASEIM AILALSKDLA DMRQRIGRVV
LAYNIDGNPI TAEDLQVAGA MTVTMCEAIE PTLMQTLEGV ATLIHAGPFA NIAHGNSSII
ADRIALKLSE FTVTEGGFGS DMGFEKACNI KAQQADRGPD CAVVVATLRG LKANSGLYDL
RPGQALPDAI FSPDEKALIA GFDNLKWHIR NAAQYGLPVV VAINRFPQDT DVELELLKNM
VADTDFSTYV GVAISEAFGK GGEGATELAQ AVVKACETPA NFKPLYSLSQ SLEEKLMAVA
EVGYGARSIE LSDCAKEQLA TLKKHGHDNL AVCLAKTPLS ITTDPGIKGA PSDFVVPVRE
LKLCAGAGFV YALCGNVMTM PGLPEKPAYM NLDIDADGNI VGLS
