FTHS_METRJ
ID FTHS_METRJ Reviewed; 557 AA.
AC B1M0D1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
GN OrderedLocusNames=Mrad2831_4072;
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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; CP001001; ACB26042.1; -; Genomic_DNA.
DR RefSeq; WP_012320998.1; NC_010505.1.
DR AlphaFoldDB; B1M0D1; -.
DR SMR; B1M0D1; -.
DR STRING; 426355.Mrad2831_4072; -.
DR EnsemblBacteria; ACB26042; ACB26042; Mrad2831_4072.
DR KEGG; mrd:Mrad2831_4072; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006589; 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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000196816"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 59349 MW; 809722BF98FD83CA CRC64;
MPSDIEIARA ATLKPIAQVA EKLGIPDDAL HNYGKHIAKI DHGYIAGLES RKPGKLVLVT
AISPTPAGEG KTTTTVGLGD ALNRIGEKTM ICLREPSLGP CFGMKGGAAG GGKAQVVPME
QINLHFTGDF HAITSAHSLA AALIDNHVYW ANELNIDVRR IHWRRVVDMN DRALRAITQS
LGGVANGFPR EDGFDITVAS EVMAVFCLAK DLADLEERLG RIVIAETRDR KLVTLKDVKA
TGAMTVLLKD ALQPNLVQTL EGNPALIHGG PFANIAHGCN SVIATRAGLR LADYTVTEAG
FGADLGAEKF LDIKCRQAGL TPSAVVVVAT IRALKMHGGV DKKNLGAENI DALEKGFANL
ARHVTNLRGF GLPVVVGVNH FHADTEAEHA KLKELCRERL DVEAITCRHW AEGGAGAEEL
ARAVVKLSQA EPAPIRHAYE TESRLTDKIR AIATKLYGAA DIQIETKAAG KLATFEKDGY
GHLPICMAKT QYSFSTDPTL MGAPEGHIVG VRDVRLSAGA GFVVAICGEI MTMPGLPRVP
AADTIRLDAN GQIDGLF