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Database: UniProt
Entry: X7F4V8_9RHOB
LinkDB: X7F4V8_9RHOB
Original site: X7F4V8_9RHOB 
ID   X7F4V8_9RHOB            Unreviewed;       558 AA.
AC   X7F4V8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000256|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000256|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN   ORFNames=RISW2_16560 {ECO:0000313|EMBL:ETX27079.1};
OS   Roseivivax isoporae LMG 25204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27079.1, ECO:0000313|Proteomes:UP000023430};
RN   [1] {ECO:0000313|EMBL:ETX27079.1, ECO:0000313|Proteomes:UP000023430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27079.1,
RC   ECO:0000313|Proteomes:UP000023430};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01543}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETX27079.1}.
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DR   EMBL; JAME01000041; ETX27079.1; -; Genomic_DNA.
DR   RefSeq; WP_043774227.1; NZ_JAME01000041.1.
DR   AlphaFoldDB; X7F4V8; -.
DR   STRING; 1449351.RISW2_16560; -.
DR   PATRIC; fig|1449351.3.peg.3995; -.
DR   eggNOG; COG2759; Bacteria.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000023430; Unassembled WGS sequence.
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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01543, ECO:0000313|EMBL:ETX27079.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01543}; Reference proteome {ECO:0000313|Proteomes:UP000023430}.
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   558 AA;  59179 MW;  7096C20A5039A92A CRC64;
     MAFKTDIEIA RAARKRPIQE IGETLGIASE HLLPYGHDKA KVSQAFIDSL ADRPDGKLIL
     VTAINPTPAG EGKTTTTVGL GDGLNAIGRK ACICIREASL GPNFGMKGGA AGGGYAQVVP
     MEEMNLHFTG DFHAITSAHN LLAAMIDNHV YWGNEQDIDV RRVTWRRVLD MNDRALRQIT
     ASLGGVANGF PREAGFDITV ASEVMAILCL ARDLADLQER LGAMIAAYRR DKTPVFARDL
     KADGAMTVLL KDAMQPNLVQ TLENNPAFVH GGPFANIAHG CNSVIATRTA LKLADYVVTE
     AGFGADLGAE KFMNIKCRKA GLAPDCVVVV ATVRAMKMNG GVAKADLGAE NVAAVEAGCA
     NLGRHIENVK GFGVPVVVGI NHFAGDTEAE IAAVRAYVAA QGAEAILCRH WAEGSKGMTE
     MAARVAEIAD AGTSAFRTLY PDEMGLMEKI ETVAKRIYRA GSVTADARVR AQLKDWEAQG
     YGALPVCMAK TQYSFSTDPG ARGAPEGFDL PVREVRLSAG AGFVVAICGE IMTMPGLPRV
     PSAESIRLNA QGQIEGLF
//
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