FTHS_ALISL
ID FTHS_ALISL Reviewed; 554 AA.
AC B6EIJ9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=VSAL_I2184;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ79869.1; -; Genomic_DNA.
DR RefSeq; WP_012550701.1; NC_011312.1.
DR AlphaFoldDB; B6EIJ9; -.
DR SMR; B6EIJ9; -.
DR STRING; 316275.VSAL_I2184; -.
DR EnsemblBacteria; CAQ79869; CAQ79869; VSAL_I2184.
DR KEGG; vsa:VSAL_I2184; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001730; Chromosome 1.
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 Gene3D; 3.40.50.300; -; 3.
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.
FT CHAIN 1..554
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000146671"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 554 AA; 59636 MW; E33BF504A82F5E27 CRC64;
MKSDIEICQT ATLIRMKTIA SNLGLHDDDI TPQGRYKAKV NIDALKHLED KPSGKLILVT
AITPTPLGEG KTVTTIGLAQ GLAKLGESVS ACIRQPSMGP VFGVKGGAAG GGYSQVAPME
ELNLHLTGDI HAITAAHNLA SAAIDARIYH EQRLGYNIFS EKNDLPALRI DPTQVVWKRV
MDHNDRALRM VTIGKNEDNK TINGYEREDG FDITAASELM AILALATDLQ DLRQRIGRIV
VAYNLDGLPI TTEDLQVAGA MTVTMKFAIN PTLMQTLEGV PTFVHSGPFA NIAHGNSSII
ADNIALKLTD YTVLVATLRG IKANSGLFPL SSGQSLPKAL FVPNQEALIA GLDNLHWHIK
NCAKYGLPVV VAINRFPEDT QEELDFLADW VTSQSSELNL DVAISEAFGK GGEGTRELAQ
KVLIACAQET EFTPLYTPDM SLLDKLTAVA IKGYGAERLE LSEKAQQQLA MFEQLGYQHL
SVCMAKTPAS ISTDGNIKGA PTDFIVPIRE LRLCAGAGFV YALCGNVMTM PGLPEKPAFM
NLDIDSNGNI TGLS
