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Database: UniProt
Entry: A0A1Y5SY32_9RHOB
LinkDB: A0A1Y5SY32_9RHOB
Original site: A0A1Y5SY32_9RHOB 
ID   A0A1Y5SY32_9RHOB        Unreviewed;       558 AA.
AC   A0A1Y5SY32;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ECO:0000313|EMBL:SLN50893.1};
GN   ORFNames=ROA7023_02215 {ECO:0000313|EMBL:SLN50893.1};
OS   Roseisalinus antarcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseisalinus.
OX   NCBI_TaxID=254357 {ECO:0000313|EMBL:SLN50893.1, ECO:0000313|Proteomes:UP000193900};
RN   [1] {ECO:0000313|EMBL:SLN50893.1, ECO:0000313|Proteomes:UP000193900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7023 {ECO:0000313|EMBL:SLN50893.1,
RC   ECO:0000313|Proteomes:UP000193900};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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}.
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DR   EMBL; FWFZ01000009; SLN50893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SY32; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000193900; 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.
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:SLN50893.1};
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:UP000193900}.
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;  59113 MW;  8DA9CD9881AA63F5 CRC64;
     MAHQTDIEIA RAAHKLPIQE IGAKLGIGAE DLVPYGHDKA KVSQRLIESV RNHATGKLIL
     VTAINPTPAG EGKTTTTVGL GDGLNRIGQR AAVCIREASL GPNFGMKGGA AGGGHAQIVP
     MEDMNLHFTG DFHAITSAHN LLSAMIDNHI YWGNGLEIDQ RRVVWRRVLD MNDRALRDTV
     TSLGGVSNGF PRQTGFDITV ASEVMAILCL ATSLGDLERR LGDMIVAYRR DKSPVTARDI
     KADGAMTVLL KDALQPNLVQ TLENNPAFVH GGPFANIAHG CNSVMATTTA LKLADYVVTE
     AGFGADLGAE KFMDIKCRKA GLSPDAVVLV ATCRAIKMNG GVAKDDLGQE NVAAIEAGCP
     NVGRHIANLA QFGVPVVVAI NHFLGDTEAE LAAVKAYVAE QGVEAILCTH WAQGGAGTEA
     LARKVVEMAE GGTAQFAPLY PDEMPLWEKI ETIATRIYHA GEVTADKSVR AQLAAWEAEG
     HGHLPICMAK TQYSFSTDPA RRGAPSGHSV PVREVRLAAG AGFIVVICGE IMTMPGLPRV
     PSAESIRLNA EGLIEGLF
//
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