FTHS_ACICJ
ID FTHS_ACICJ Reviewed; 557 AA.
AC A5G276;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Acry_2767;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
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 Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ31958.1; -; Genomic_DNA.
DR RefSeq; WP_012040297.1; NC_009484.1.
DR AlphaFoldDB; A5G276; -.
DR SMR; A5G276; -.
DR STRING; 349163.Acry_2767; -.
DR EnsemblBacteria; ABQ31958; ABQ31958; Acry_2767.
DR KEGG; acr:Acry_2767; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000245; 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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000068787"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 58079 MW; 3DAD16EE4068CE7E CRC64;
MASDLDIARA SRLRPIGEIA AAAGIPAEAL IPYGRYKGKV DGGFIRSLED RPDGALVLVV
GISPTPAGEG KTTTSIGLGD ALRAAGAKAM IALREPSLGP CFGQKGGATG GGRAQVAPME
EINLHFTGDF HAITSANNLL AAMLDNHVYW GNELGIDPRR IAFRRAIDMN DRALRQTVLG
LGDGANGAAR EQKFDITVAS EVMAIFCLAR DLDDLQRRLA RIVVAERRDG SPVTPADLKA
VGAMAALLRD ALQPNLVQTL EGTPALVHGG PFANIAHGCN SVIATRTALK LADIVVTEAG
FGADLGGEKF LDIKCRQAGL APSCAVVVAT IRALKMHAGV AKADLGAENP GAVARGAANL
RRHVAAMRAF GLPVIVAING FVTDTGAERE ALRAALDEDG GARICFCTHW ADGSAGATDL
AQAVIETIAA KSARFAPLYP DDMKLPHKLR TIAQRIYGAD DIELSPLAAK RLARFEAQGY
DHLPVCVAKT QYSFTADPAR RGAPTGFTVP IRDARLSAGA GFVVALAGDV MTMPGLPRIP
AAEAIGLDPD GAIHGLF
