FTHS_MALP2
ID FTHS_MALP2 Reviewed; 530 AA.
AC Q8EUQ1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=MYPE8690;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC44661.1; -; Genomic_DNA.
DR RefSeq; WP_011077690.1; NC_004432.1.
DR AlphaFoldDB; Q8EUQ1; -.
DR SMR; Q8EUQ1; -.
DR STRING; 272633.26454332; -.
DR EnsemblBacteria; BAC44661; BAC44661; BAC44661.
DR KEGG; mpe:MYPE8690; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_14; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002522; 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 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..530
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199362"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 530 AA; 59817 MW; 2F9A209EA3D87C9A CRC64;
MTNNIFKYFN IKELEKFGKF YKVKKEYEIP KKLESKLILV TSINPTPEGE GKTTTLIGIN
DCLNYFGKES IACLRQPSMG PYFGIKGGAT GSGKCEIQNP EKVNCGFTND FYAIEAANNL
IMSVIENEIY FNTDLEIDPQ KIIWKRCIDI NDRSLRDINY QVSKNTKINS SFSITAASNL
MALFCLAKSK SDFKKRIENT LVAFSKSNKA IYVKDLNIID SIMLILDDAL KPNLVFSQDN
NPIIMHGGPF ANIAHGCNSV IALSCGLNKA EYVLTEAGFG SELGAEKFIN ILCRETNLVP
NLVVLTITLK AIKYHGVNNS NNTSPLTDEK EKIDIGFNNV IHHFNLLKNL NLNVCIVINK
FSDDNKNELD YLFNKSSELT KTVISTMWQD GASKNKSLFE TIIESVQEPK PINWTYDLKD
NAVNKINDLS TKVYNGATIT YSDLATAKLK DNENWIQDYY VCGAKTPYSP SIKNEYMDTN
KHDIHVEDIE INHAVKFIIP IFSKTFLMPG LPKVPNAKKI KINFDKFKYE
