ID   FTHS_SPHSK              Reviewed;         558 AA.
AC   O66164; G2IQS9; Q60FW9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   24-JAN-2024, entry version 76.
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   Synonyms=ligH {ECO:0000303|PubMed:9501423};
GN   ORFNames=SLG_12760 {ECO:0000312|EMBL:BAK65951.1};
OS   Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=9501423; DOI=10.1128/aem.64.3.836-842.1998;
RA   Nishikawa S., Sonoki T., Kasahara T., Obi T., Kubota S., Kawai S.,
RA   Morohoshi N., Katayama Y.;
RT   "Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene
RT   essential for the O demethylation of vanillate and syringate.";
RL   Appl. Environ. Microbiol. 64:836-842(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=15743951; DOI=10.1128/jb.187.6.2030-2037.2005;
RA   Abe T., Masai E., Miyauchi K., Katayama Y., Fukuda M.;
RT   "A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for
RT   catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6.";
RL   J. Bacteriol. 187:2030-2037(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=22207743; DOI=10.1128/jb.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(2012).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=15090517; DOI=10.1128/jb.186.9.2757-2765.2004;
RA   Masai E., Sasaki M., Minakawa Y., Abe T., Sonoki T., Miyauchi K.,
RA   Katayama Y., Fukuda M.;
RT   "A novel tetrahydrofolate-dependent O-demethylase gene is essential for
RT   growth of Sphingomonas paucimobilis SYK-6 with syringate.";
RL   J. Bacteriol. 186:2757-2765(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cannot degrade vanillate or syringate, but
CC       it can degrade protocatechuate and 3-O-methylgallate (PubMed:9501423).
CC       Mutant shows O-demethylation activity toward both vanillate and
CC       syringate in the presence of tetrahydrofolate, indicating that ligH is
CC       not directly involved in the O demethylation of vanillate and syringate
CC       (PubMed:15090517). {ECO:0000269|PubMed:15090517,
CC       ECO:0000269|PubMed:9501423}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR   EMBL; AB006079; BAA25140.1; -; Genomic_DNA.
DR   EMBL; AB186750; BAD61061.1; -; Genomic_DNA.
DR   EMBL; AP012222; BAK65951.1; -; Genomic_DNA.
DR   RefSeq; WP_014075602.1; NC_015976.1.
DR   AlphaFoldDB; O66164; -.
DR   SMR; O66164; -.
DR   STRING; 627192.SLG_12760; -.
DR   KEGG; ssy:SLG_12760; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001275; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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"
FT                   /id="PRO_0000199370"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
FT   CONFLICT        13..14
FT                   /note="AK -> ER (in Ref. 1; BAA25140)"
FT   CONFLICT        175..176
FT                   /note="AL -> V (in Ref. 1; BAA25140)"
FT   CONFLICT        427
FT                   /note="L -> H (in Ref. 1; BAA25140)"
SQ   SEQUENCE   558 AA;  59464 MW;  1DEA902749928A65 CRC64;
     MAQGSDIEIA REAKMQNIAE VGAKVGIPQD ALLNYGPYKA KLSWDFINSV QGNQDGKLIL
     VTAINPTPAG EGKTTTTVGL ADGLNRIGKK TVAALREPSL GPCFGVKGGA AGGGYAQVVP
     MEDINLHFTG DFHAITSANN LLAALIDNHI YWGNKLGLDP RRIAWRRVLD MNDRALRSIV
     NSLGGVSNGY PREDGFDITV ASEVMAILCL SSDLKDLERR LGNIHAGYTR ERKAVLASEL
     NASGAMTVLL KDALQPNMVQ TLENNPVLIH GGPFANIAHG CNSVLATKTA LKIADYVVTE
     AGFGADLGAE KFFDIKCRKA GLKPSAAVIV ATIRALKMHG GVDKADLGTA NPEAVRKGGV
     NLARHIENVR QFGVPVVVAI NQFITDTDEE MAMVKEIAEA AGAEAVLCSH WANGSAGTEE
     LARKVVLHAE SGSSNFAPLY EDSMPLFEKI DTIAKRIYRA TEATADSSVR NKLKGWEADG
     FGHLPVCMAK TQYSFSTDPA LRGAPTDHVV PVRDVILSAG AEFIVAVCGD IMRMPGLPKV
     PSADFIKLDE QGQIQGLF
//