FTHS_SYNAS
ID FTHS_SYNAS Reviewed; 565 AA.
AC Q2LU82;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SYNAS_17640;
GN ORFNames=SYN_02008;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77643.1; -; Genomic_DNA.
DR RefSeq; WP_011417665.1; NC_007759.1.
DR AlphaFoldDB; Q2LU82; -.
DR SMR; Q2LU82; -.
DR STRING; 56780.SYN_02008; -.
DR PRIDE; Q2LU82; -.
DR EnsemblBacteria; ABC77643; ABC77643; SYN_02008.
DR KEGG; sat:SYN_02008; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001933; 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..565
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293072"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 565 AA; 60940 MW; B4CF77DEDE1BFDE1 CRC64;
MTHRNSRQDT KELKPIADIA ATIGLSEDDI EAYGRYKAKV RLEAISRFHS RPDASLILVS
AMTPTPAGEG KTTVSIGLAQ ALARLGKATI AALREPSLGP VFGMKGGATG GGLSRVHPVD
DINLHFTNDF AAVESAHNLL SAIVDNSVYH DNILNIDPRK VTWRRVLDMN DRFLRNIVIG
LGGSVNGVPR ETGFDIVPSS EIMAILCLSR SYRELKEKIR RILVGFTYDD SPVMAGDLKV
EGAVTALLKY ALLPNLVQTT ENVPAIIHGG PFANIAQGTS SILGTDLALR LADYVVTEAG
FGFDLGAEKF FDIVAPYGGL NPRIVVLVAT VRALKYHAGI AQADLDRSNP RAAVLGMANL
RKHYQNIDKF HVSCVIALNR FSSDTDEEIN AVVRAAENEG MNIAPCDIFR LGGEGGLELA
EKTLELLAGT SCGYRRLYEW NQPVEDKIFT VASEIYGAVS IDYQPLARRN LDLINKYGFD
KLPVCIAKTQ QSLSDNPGLL GLPRDFIVTV REIRIASGAG FLIPITGEIL RMPGLSKRPA
AYSIDIDDSG NITGVGSPGG ISSLS
