FTHS_PSYWF
ID FTHS_PSYWF Reviewed; 569 AA.
AC A5WI04;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543};
GN OrderedLocusNames=PsycPRwf_2355;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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; CP000713; ABQ95295.1; -; Genomic_DNA.
DR RefSeq; WP_011961566.1; NC_009524.1.
DR AlphaFoldDB; A5WI04; -.
DR SMR; A5WI04; -.
DR STRING; 349106.PsycPRwf_2355; -.
DR EnsemblBacteria; ABQ95295; ABQ95295; PsycPRwf_2355.
DR KEGG; prw:PsycPRwf_2355; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
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.
FT CHAIN 1..569
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000073556"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 569 AA; 60834 MW; 2EC061E82362AE3B CRC64;
MTVPSDITIA QNATLRPIVD IAKKIGLSAD KIEPYGYYKA KINPNDVFDM PAKSSNSKLV
LVTAINPTPA GEGKTTVTIG LADALNRVHH QDQNGKRTVV ALREPSVGPV FGIKGGAAGG
GYAQVLPMED INLHFTGDLH AIGAANNLLA ALIDNHIYQG NALNIDPKQV VWRRAVDMND
RQLRNTVTGL GKPADGVMRE DGFDITVASE VMAIFCLATD LADLKQRLGN ILVAYNQDKQ
PIYAKDLKAH GAMAALLKDA IKPNLVQTIE GTPAILHGGP FANIAHGCNS VIATRTAMHL
ADYTLTEAGF GADLGAEKFC DIKCRLAGLT PDAAVVVATI RALKYNGGAA KDALKNEDLT
ALEQGLPNLT KHIENLQEVF GLPVVVAINQ FESDTAAEIE MVRKACKRLK VEVALTQVWE
KGGAGGEDLA RTLLALLETH NDQPQTFGFA YDSNKPIVNK IRTVAQRIYG ANDVDISVTA
AAKIKRLEAL GLDKMPICIA KTQYSLSDDA KLLGRPTGFN IHVRDISVSN GAGFIVVICG
PIMKMPGLPK YPSAENIDVD EKGNITGLF
