FTHS_PORGI
ID FTHS_PORGI Reviewed; 555 AA.
AC Q7MUZ8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=PG_1321;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ66392.1; -; Genomic_DNA.
DR RefSeq; WP_004585540.1; NC_002950.2.
DR AlphaFoldDB; Q7MUZ8; -.
DR SMR; Q7MUZ8; -.
DR STRING; 242619.PG_1321; -.
DR EnsemblBacteria; AAQ66392; AAQ66392; PG_1321.
DR GeneID; 29256317; -.
DR KEGG; pgi:PG_1321; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_10; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000588; 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..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199368"
SQ SEQUENCE 555 AA; 60075 MW; 900DD71B42D28A9F CRC64;
MKSDIQIARD IELQRIEQIA ESIDLPVEQL EPYGRYTAKV PLSCIDEEKV KKGNLILVTA
ITPNKAGVGK TTVSIGLALG LNHIGKKAIV ALREPSLGPC FGMKGGAAGG GYAQVLPMEN
INLHFTGDFH AVTSAHNMIT ALLENYIYQN RNTCDGLSEI LWKRVLDVND RSLRNAVTGL
GTISDGIPRQ TGFDITPASE IMAILCLAKD FEDLRSRLEN ILLGYTKEGA PFTVKDLGIA
GSIAVLLKDA IKPNLVQTTE HTPAFVHGGP FANIAHGCNS ILATKMALSF GEYAVTEAGF
GADLGAEKFL DIKCREMGVA PKLTVLVATL RALKLHGGVA ETEIKAPNAE ALRRGLSNLD
RHIYNLKKFG QQVIVAFNRF DTDEEEEISI VREHCIGQNV GFAVNNAFAE GGKGAEELAK
LVVEMVENKP SQPLKYAYEP ENPVKMKIEK IAKEIYSAGS VVYSSKADGK LKKIAMQSLD
HLPVCIAKTQ YSFSSDPKAK GDVRGFELKV SDIIINRGAG MLVVIIGEIM RMPGLPKEPQ
AVHIDIVDGF IEGLS
