FTHS_MYXXD
ID FTHS_MYXXD Reviewed; 551 AA.
AC Q1DFW5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, 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=MXAN_0175;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF87836.1; -; Genomic_DNA.
DR RefSeq; WP_011550322.1; NC_008095.1.
DR AlphaFoldDB; Q1DFW5; -.
DR SMR; Q1DFW5; -.
DR STRING; 246197.MXAN_0175; -.
DR PRIDE; Q1DFW5; -.
DR EnsemblBacteria; ABF87836; ABF87836; MXAN_0175.
DR GeneID; 41357678; -.
DR KEGG; mxa:MXAN_0175; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002402; 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; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293048"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 551 AA; 58072 MW; 67F9271C23228902 CRC64;
MTLRAMTDVG AELGLSPEDV LPWGTHRAKV SLDALGKRGG RQGRLVLVSA INPTPPGEGK
TTMSVALAMG LRKRGRRAVA ALREPSLGPV FGVKGGGTGG GQASLEPAAD INLHFTGDLH
AITSANNLLS ALVDNAVFYG QPVALDATRV RWRRALDMND RFLRNVIVGL GGKAQGVPRE
DHFDITAASE VMAILALAEG LKDLEARLGR VIIGHTRDGQ PVRARDVDAA ASMVALLKDA
LMPNLAQTRE GGPALVHAGP FANIAHGCSS VMGTRMGLAY ADEVITEAGF GFDLGAEKFL
DIKCRGSGLW PRGVVLVVTL RALKHHGGAS PARVAEPDRE ALVRGFAHLE KHLESVAAFG
LPAVLCVNRF PQDTESELEE LRAFGKARGV ETAVCDGFSR GGDGSLELAD CVLEMLDGTD
AAPPQPRFLY DVAQTPEEKV AAIARTVYGA DDVAFTASAK KDLDAIRELG GAGLPVCMAK
THLSLSDDPT KLGRPRGFTL TVREVRLSAG AGFMVALTGE ILTMPGLPRE PAARRVTVHD
DGRVTGLMQG E