FTHS_CUTAK
ID FTHS_CUTAK Reviewed; 563 AA.
AC Q6ABS5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=PPA0049;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT81808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017283; AAT81808.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6ABS5; -.
DR SMR; Q6ABS5; -.
DR STRING; 267747.PPA0049; -.
DR EnsemblBacteria; AAT81808; AAT81808; PPA0049.
DR KEGG; pac:PPA0049; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000603; 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.
FT CHAIN 1..563
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199369"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 563 AA; 59660 MW; 6BE2573EA8575BA1 CRC64;
MKSDLEIARE AHLDPIEKVA ARAGIDEKYL EPYGRGVAKV DLDVVTHNRD HSCGKYVVVT
AMTPTPLGEG KTTTAVGLAQ GLEKIGKHSV LALRQPSMGP TFGIKGGAAG AGYSQVLPME
KLNLHLTGDF HAIGAAHNLL AAMIDNHLHQ GNELDIEPHS ISWRRVVDIN DRALRNTIVG
LGSRVDGVPR ETGFDITAAS EVGVILSLAT SLSDLRARLG RIVIGYNRSK EPVSAEDLHA
AGSMAVILKD ALKPNLLQTT ENSPVLVHAG PFGNIATGNS SVIADRVGIG CGDYLLTEAG
FGADMGAERF FNIKCRIGGM RPDAAVLVAT VRALKTHAGR YKVIPGKPLP PAMLEDNPDD
VLAGAANLRK HIEIVREFGV SPIVALNVFP TDHPDEIDAV RKVAEAAGAH FASSTHVVDG
GDGAVDLAHA VVAACDHKAD FRYTYDLEDS LVEKLTKVAT KVYGADGIDI APAAAKELAH
FEDLGYGTFP VVIAKTHLSL SHDPSLKGAP TGWRLPVREV RAAVGAGYIY AICGDMRTMP
GLGRHPAAER IDIDDNGETI GLF
