FTHS_AERS4
ID FTHS_AERS4 Reviewed; 580 AA.
AC A4SPE5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=ASA_2749;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO90767.1; -; Genomic_DNA.
DR RefSeq; WP_005309936.1; NC_009348.1.
DR AlphaFoldDB; A4SPE5; -.
DR SMR; A4SPE5; -.
DR STRING; 382245.ASA_2749; -.
DR EnsemblBacteria; ABO90767; ABO90767; ASA_2749.
DR KEGG; asa:ASA_2749; -.
DR PATRIC; fig|382245.13.peg.2724; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000225; 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; 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..580
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300515"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 580 AA; 60953 MW; 3E6AFCE1DCF8BBA2 CRC64;
MLSDIEISRQ SPRLSIQALA SRLGIPAHLL SPHGHYKGKL SLELLKQAAS KPGKKAGKLV
LVSAITPTPL GEGKTVTTLG LSMGLNHIGQ PSMATIRQPS LGPVFGVKGG AAGGGHAQVV
PMEEMNLHLT GDFHALTAAH NLAAAALDAR LFHETKLGTE FTARTGLARL DIDPANILWP
RTLDMNERAL RHLTIGQGAA ADGVERQDRF VITAASELMA ILALASDLKD LRARIGRIQL
ALDSQGQPIT AEQLEVAGAM TVLLKDALQP TLMQTTEQTP VLVHAGPFAN IAHGNSSVIA
DRMALQLTDY VVTEAGFGSD MGLEKFFNIK HRQSGITPAC VVLVATVRGL KANSGLLDIR
PGQPLPASLL GEDLPTLEKG CANLAWHIHN ARRYGLPVVV AVNSFPTDSK AELDLLMREA
RQAGACGAAI STAFVEGGAG ASELARAVVA ACEMPSQIQL LYPDEMSLCA KLATLVECGY
GGRGVILSDK AHRQLAALSA AGWDHLPICV AKTPLSISHD PARKGVPTDF EVPIDEVKLC
AGAGFVYALA GPIMTMPGLG SLPAYRHIDI GEDGEIVGLS
