FTHS_SPHSK
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 03-AUG-2022, entry version 71.
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; Proteobacteria; 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 = (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 -!- 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 EnsemblBacteria; BAK65951; BAK65951; SLG_12760.
DR KEGG; ssy:SLG_12760; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OrthoDB; 177859at2; -.
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; 3.40.50.300; -; 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"
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