FTHS3_RUBXD
ID FTHS3_RUBXD Reviewed; 573 AA.
AC Q1AT39;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Formate--tetrahydrofolate ligase 3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 3 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs3 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=Rxyl_2519;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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; CP000386; ABG05439.1; -; Genomic_DNA.
DR RefSeq; WP_011565449.1; NC_008148.1.
DR AlphaFoldDB; Q1AT39; -.
DR SMR; Q1AT39; -.
DR STRING; 266117.Rxyl_2519; -.
DR EnsemblBacteria; ABG05439; ABG05439; Rxyl_2519.
DR KEGG; rxy:Rxyl_2519; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OrthoDB; 177859at2; -.
DR PhylomeDB; Q1AT39; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006637; 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;
KW Reference proteome.
FT CHAIN 1..573
FT /note="Formate--tetrahydrofolate ligase 3"
FT /id="PRO_0000293056"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 573 AA; 61311 MW; CDAE742660E99CAF CRC64;
MLTNLEIARG AKLLPIEEVG RSMGLREERH LEPYGRHVAK VDLCAIEDLS ERPKAKYILV
SAITPTPLGE GKTTTTVGLG QAFSHIGKRA TIAIRQASMG PAFGIKGGAA GGGYSQVVPM
ERLNLHLTGD LHAVTEAHNM LAAMIDNHLY HGNGLGIEPH SISWRRVMDV NDRSLRNIVI
GLGARTDGVP RQSGFDITAA SEVMAILALA SSLEDLRERL GRIVIGHNRE GNPVSAEDVR
GAGAMAVILK EAIKPNLMQT LEGTPALVHA GPFGNIATGN SSVVADLIGI RTADYLITEA
GFGADMGAER FFNIKCRISG LEPDAAVVVA TVRALKAHSG RYQIKAGAPL PEELLEENPQ
DVLAGAENLK KQIENIKLHG VPAVVAINAF PTDHPSEHKA IEEAAKEVGA RCAVCRHFTE
GGKGAVELAR ALEETIEENE RERRRGGGGS FRFLYPLEMP LKQKIETIAR EVYGAEGVEY
DAEALRALEG FERAGFGRLP VCLAKTHLSL SSDPALKGAP RGWKLSVREV RASVGAGFIY
PICGQMRTMP GLSAHPAAER IDLDGEGNVV GLF