FTHS_PROMH
ID FTHS_PROMH Reviewed; 556 AA.
AC B4ET09;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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}; OrderedLocusNames=PMI0670;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR41561.1; -; Genomic_DNA.
DR RefSeq; WP_012367694.1; NC_010554.1.
DR AlphaFoldDB; B4ET09; -.
DR SMR; B4ET09; -.
DR STRING; 529507.PMI0670; -.
DR EnsemblBacteria; CAR41561; CAR41561; PMI0670.
DR GeneID; 6800336; -.
DR KEGG; pmr:PMI0670; -.
DR PATRIC; fig|529507.6.peg.652; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008319; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000196820"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59996 MW; 63FE610A8CA6C3E5 CRC64;
MKSDIEISHQ APLLPIQDIA KKINVDQDDI EFYGKYKAKF SQSIWSKITS KKQGKLVLVT
SINPTPAGEG KTTVTVGLGQ ALNQLGKSAI IALREPSLGP CFGLKGGAAG GGYSQVVPME
DLNLHFTGDF HAITSANNLL AAMLDNSLYQ GNPLNINPKK IIFKRCMDMN DRALRHLVIG
LGGDKDGVVR EDSFVITVAS EIMSILCLAK DINDLKQRLA RIIVAYNYEG EPVSAEDLNA
VGAMATLLKD ALNPNLVQTL ENTPAIIHGG PFANIAHGCN SLRATKLALQ LADITVTEAG
FGADLGAEKF FDIKCRIGDL QPDCAVLVVT TKALKYNGGL GKTQWDHENL TALATGIENL
GKHIENLKKY GVPVIVTVNA YVTDSAKEHE FIAQYCQQRG CRFAISQVWE KGGAGGIELA
NQVIDTLEND APQFQLLYPD NMPLKQKIET IAQEIYGAKG VTYNANAQEM LTKIEDMGFG
HFPICMAKTQ YSLSDDPALL GRPTDFTINI REVYVSAGAG FVVSLTGTIN TMPGLPKKPA
AMAMDVDDHG AIKGLF