FTHS2_DESHY
ID FTHS2_DESHY Reviewed; 558 AA.
AC Q24ZZ8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Formate--tetrahydrofolate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs2 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=DSY0605;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE82394.1; -; Genomic_DNA.
DR RefSeq; WP_005809880.1; NC_007907.1.
DR AlphaFoldDB; Q24ZZ8; -.
DR SMR; Q24ZZ8; -.
DR STRING; 138119.DSY0605; -.
DR EnsemblBacteria; BAE82394; BAE82394; DSY0605.
DR KEGG; dsy:DSY0605; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; TRQGFSK; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001946; 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..558
FT /note="Formate--tetrahydrofolate ligase 2"
FT /id="PRO_0000293035"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 558 AA; 59457 MW; 71991F4502367679 CRC64;
MAFKSDIEIA QESTMLPVAE LAEKLNIAEE YVESYGKYKA KIDYNLLKEK GNTPDGKLIL
VTAINPTPAG EGKTTTTVGL GDALTHLGKK VVIALREPSL GPVFGVKGGA AGGGYAQVVP
MEDINLHFTG DLHAIGAANN LIAALLDNHI YQGNALDIDV RRITWKRCMD MNDRQLRYIN
DGLGGKANGM PREDGFDITV ASEIMAILCL SSDLDDLKQR VERIIVGYNR KGEPVTAGQL
KAQGAVAALL KDALKPNLVQ TLEHTPSFIH GGPFANIAHG CNSVMATKMA LKLGDYVVTE
AGFGADLGAE KFLDIKCRLS GLEPDAVVIV ATVRALKSHG GVAKADLNQE NLAALKEGLP
NLLKHVENIT VNFGLPAVVA INRFPTDTLA EVQLVEEECK KLGVNVALSE VWEKGGAGGV
ELAEEVLKLM DSPKNFTFAY DIDLGLKEKI TAIATKIYGA DGVDFIGSST KDIEGIESIG
YRNIPVCMAK TQYSLSDDQK KLGRPTGFRI SIRSVKVSAG AGFAVALTGD IMTMPGLPKV
PAAESIDVDN TGRISGLF