FTHS_BRAHW
ID FTHS_BRAHW Reviewed; 553 AA.
AC C0QX38;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=BHWA1_02387;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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; CP001357; ACN84841.1; -; Genomic_DNA.
DR RefSeq; WP_012671871.1; NC_012225.1.
DR AlphaFoldDB; C0QX38; -.
DR SMR; C0QX38; -.
DR STRING; 565034.BHWA1_02387; -.
DR PRIDE; C0QX38; -.
DR EnsemblBacteria; ACN84841; ACN84841; BHWA1_02387.
DR KEGG; bhy:BHWA1_02387; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_12; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001803; 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; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT CHAIN 1..553
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000185248"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 553 AA; 59991 MW; E38F6A1EDC7E5F0D CRC64;
MKTDIEIAQE CKLERIEKIA EKLNLTDDDY EVYGKYKAKI ELSLLNKLKD KKDGKLVLVT
AITPTPAGEG KSTVTIGLTQ GLNKIGKNAV AALREPSLGP VFGIKGGACG GGYSQIVPME
DINLHFNGDF HAISSAHNLI SACIDNHIKQ GNELKIDINK IVFKRVLDMN DRALRDIVIG
LGGSENGVVR QSSFQITVSS EIMAILCLSN SLMDLKEKIG NVIFAYDIND NPLRVKDLKI
EGAACTLLKD AIKPNLVQTL ENTPVIVHGG PFANIAHGCN SILATKMALK LSDYTITEAG
FAADLGAEKF LDIKCRLAGL KPNCIVLVAT IRALKHHGGA SDINKEDIEA LTKGFENLDK
HIENMQKYNV PVVVAINKFV SDTDKEIECI TKHCESKGID ISLCEVWAKG GEGAIELSHK
VLKAASEESN YKPLYELEKS IKEKIETICK EIYSAGEVKF SNKALKMMKK IENMGFGNLP
ICISKTQKSI SDNPALLNAP KGYTLNIDEI KLASGAGFII AMAGGIIDMP GLPKIPVACN
IDIDENGKIK GLF
