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Database: UniProt
Entry: A0A1I7JPZ5_9GAMM
LinkDB: A0A1I7JPZ5_9GAMM
Original site: A0A1I7JPZ5_9GAMM 
ID   A0A1I7JPZ5_9GAMM        Unreviewed;       579 AA.
AC   A0A1I7JPZ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=SAMN04487955_111153 {ECO:0000313|EMBL:SFU87176.1};
OS   Halomonas korlensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=463301 {ECO:0000313|EMBL:SFU87176.1, ECO:0000313|Proteomes:UP000198693};
RN   [1] {ECO:0000313|Proteomes:UP000198693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6981 {ECO:0000313|Proteomes:UP000198693};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FPBP01000011; SFU87176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7JPZ5; -.
DR   STRING; 463301.SAMN04487955_111153; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000198693; 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:SFU87176.1};
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:UP000198693}.
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   579 AA;  61320 MW;  A9515CD86B5F80F1 CRC64;
     MAPQATEPAA PRPADNLSIA RAVRLWPIEE IAHRLGLSGE VVEPYGRGIA KLDLAAMTSL
     AERPRGRYVV VTSMTPTPPG EGKTTTAIGL VQGLQRLGHI ASVALRQPSM GPTLGLKGGA
     TGGGYSQVLP MERINLHLTG DIHAVGAAHN LLAAMVDNHL HHRLEPELDP REVRWQRVID
     LNDRALRHLV LGIGGRGDGF PRQGGFEITA ASEVMAVLAL ADSLADLRRR LGRLIVGLDR
     AGEPVTAEQV GAAGAMTVLL KEALKPNLLQ TLEHAPALIH AGPFGNIAHG NSSVVADHIG
     LHASDFLVTE AGFGADMGAE RFFNIKCRAS GLAPDAAVLV VTVRALKYHS GRHRVVPGQP
     LPASLLGESP DEVREGGANL LKQIDNVRAH GLTPVVAINA FPSDHQSEHT AIRELCASVG
     VRAEVSTHAR DGGEGALGLA QALIETMNEA DEAGSGFHFL YPADLPLAAK IERIATRLYG
     AEGVDFAPGV RERLETWQRQ DYGTFPVCIA KTHMSLSHDA SRLGAPTGWR LPVREVRLSA
     GAGFVYALAG DIRTMPGLSA SPAATRLDID EDGETVGLY
//
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