FTHS2_RUBXD
ID FTHS2_RUBXD Reviewed; 576 AA.
AC Q1AVP8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Formate--tetrahydrofolate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs2 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=Rxyl_1568;
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; ABG04530.1; -; Genomic_DNA.
DR RefSeq; WP_011564547.1; NC_008148.1.
DR AlphaFoldDB; Q1AVP8; -.
DR SMR; Q1AVP8; -.
DR STRING; 266117.Rxyl_1568; -.
DR EnsemblBacteria; ABG04530; ABG04530; Rxyl_1568.
DR KEGG; rxy:Rxyl_1568; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR PhylomeDB; Q1AVP8; -.
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..576
FT /note="Formate--tetrahydrofolate ligase 2"
FT /id="PRO_0000293055"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 576 AA; 61555 MW; 60FF8BCC619CD358 CRC64;
MGEALSNLEI ARGAKLLPIE EVGRSMGLRE ERHLEPYGRH VAKVDLCAIE DLSERPKAKY
ILVSAITPTP LGEGKTTTTV GLGQAFSHIG KRATIAIRQA SMGPAFGIKG GAAGGGYSQV
VPMERLNLHL TGDLHAVTEA HNMLAAMIDN HLYHGNGLGI EPHSISWRRV MDVNDRSLRN
IVIGLGARTD GVPRQSGFDI TAASEVMAIL ALASSLEDLR ERLGRIVIGH DREGNPVSAE
DVRGAGAMAV ILKEAIKPNL MQTLEGTPAL VHAGPFGNIA TGNSSVVADL IGIRTADYLI
TEAGFGADMG AERFFNIKCR ISGLEPDAAV VVATVRALKA HSGRYQIKAG APLPEELLEE
NPQDVLAGAE NLKKQIENIK LHGVPAVVAI NAFPTDHPSE HKAIEEAAKE VGARCAVCRH
FTEGGKGAVE LARALEETIE ENERERRRGG GGSFRFLYPL EMPLKQKIET IAREVYGAEG
VEYDAEALRA LEGFERAGFG RLPVCLAKTH LSLSSDPALK GAPRGWKLSV REVRASVGAG
FIYPICGQMR TMPGLSAHPA AERIDLDGEG NVVGLF