FTHS_CORJK
ID FTHS_CORJK Reviewed; 562 AA.
AC Q4JVW2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=jk0881;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37045.1; -; Genomic_DNA.
DR RefSeq; WP_011273471.1; NC_007164.1.
DR AlphaFoldDB; Q4JVW2; -.
DR SMR; Q4JVW2; -.
DR STRING; 306537.jk0881; -.
DR EnsemblBacteria; CAI37045; CAI37045; jk0881.
DR KEGG; cjk:jk0881; -.
DR PATRIC; fig|306537.10.peg.893; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000545; 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.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..562
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199343"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 562 AA; 58634 MW; 7CF7496392C041F4 CRC64;
MTNSSATSNP QPSDVEIAQA HTLEPITTIA ERAGIPEAAL IPYGRTKAKI DVPALRAERE
GVNKKGKLVL VTAMSPTPAG EGKSTVLIGL ADAVRTAGRQ TMVAIREPSQ GPVMGIKGGA
AGGGYAQIVP MEDINLHFTG DMHAITAATN TLAAMVDNHV QHGNALGIDP RRVTWRRCLD
VNDRSLRHVV TGLGGPGQGT PREGGFDITA ASEIMAILCL ATDLEDLKKR IGRIVVGQTY
DRRPVTAGDL KCAGAITALL RDAINPNLVQ TLGGTPALVH GGPFANIAHG CNSLIATTTA
LDLSEVVLTE AGFGSDLGAE KFFDIKSRAG DLDVAATVVV ATIRSLKHNG DSVLKAGLAN
LERHVSNIRK FGVEPVVALN LFSSDTAAER SMVADWGEQF GVRVVECSVW AEGGAGAADL
ATAVLEVVDG VSDEDASSSS HQIYQPVDGV EATLHTLATE IYGAADVQFG PQALKDLAFL
KDNGWDKLPV CVSKTQYSFS DDPSALGAPS GHTLHVRELV PRIGAGFVVA LTGDVMTLPG
LPKKPAAERI DVNAQGVISG LF