FTHS_SYNFM
ID FTHS_SYNFM Reviewed; 587 AA.
AC A0LLR3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Sfum_2687;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK18365.1; -; Genomic_DNA.
DR RefSeq; WP_011699532.1; NC_008554.1.
DR AlphaFoldDB; A0LLR3; -.
DR SMR; A0LLR3; -.
DR STRING; 335543.Sfum_2687; -.
DR EnsemblBacteria; ABK18365; ABK18365; Sfum_2687.
DR KEGG; sfu:Sfum_2687; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001784; 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; IPR027417; P-loop_NTPase.
DR Pfam; PF01268; FTHFS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..587
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293071"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 587 AA; 64624 MW; 174E693ECDA3007E CRC64;
MPYDATKMMD WQISEEAEKD MPSPWQWQEK LGLLKEEILP MGRLCKLDFL KIMNRLKDKP
DGKYIEVTAI TPTPLGEGKS TTSVGLMEGL GKRGVNVGGC LRQPSGGPTM NIKGTAAGGG
NALLIPMTEF SMGLTGDIND IMNAHNLAMV ALTARMQHER NYTDEQLDRL TKMRRLHIDP
TRVEMGWIMD FCAQALRNII IGIGGRQDGY MMQSKFGIAV SSELMAILSI VKDLPDLRKR
LNEITVAFDR RGNPVTTGDL EVGGAMTAFM RNTINPTLMC TAEYQPCMVH AGPFANIAVG
QSSIIADRIG LKMFDYHVTE SGFAADIGFE KFWNVKCRYS GLKPHVSVLT TTIRALKMHG
GGPKVVAGLA MPEEYTKENL KLLEKGIVNM VHHINTIRKS GMNPVVCINA FHTDTKDEIA
LVRKHAEAAG ARCALSEHWA KGGEGALEFA DAVIDACKQE SQFKFLYPLE MKLRDRVSTV
AREVYGADGV SWTPDAEAKA KMLENDPKYD DYATMMVKTH LSLTHDPSVK GVPKGWVLPI
RDVLIYSGAK FLCPCAGTIS LMPGTSSNPA FRRIDVDVNT GKVKGLF