FTHS_VIBPA
ID FTHS_VIBPA Reviewed; 582 AA.
AC Q87HX2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=VPA0834;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000032; BAC62177.1; -; Genomic_DNA.
DR RefSeq; NP_800344.1; NC_004605.1.
DR RefSeq; WP_005479111.1; NC_004605.1.
DR AlphaFoldDB; Q87HX2; -.
DR SMR; Q87HX2; -.
DR STRING; 223926.28809069; -.
DR EnsemblBacteria; BAC62177; BAC62177; BAC62177.
DR GeneID; 1191523; -.
DR KEGG; vpa:VPA0834; -.
DR PATRIC; fig|223926.6.peg.3764; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002493; Chromosome 2.
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..582
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199409"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 582 AA; 62338 MW; E8D2B79BE66F57D0 CRC64;
MQSDIEICRN TPLSSIDVIA EKAGLLPEEF DTHGKYKAKV HPKCLARLND NQNGKLVLVT
AITPTPLGEG KTVTTIGLAQ GLAKLKQSVM ACIRQPSMGP VFGIKGGAAG GGYSQVAPME
ELNLHLTGDI HAVTAAHNLA SAALDARLFH EQREGYDAFE ARTGLKALKI DVESITWKRV
MDHNDRALRM VKIGLNEHGK TINGFERNEG FDISAASELM AIIALAKNLK DLRQRIGKIV
VAYDLDGQPI TTEDLQVAGA MAVTLKEAIA PTLMQTLEGV PTLIHAGPFA NIAHGNSSII
ADEIALKLSR YTVTEAGFGS DMGFEKACNI KAAAANKAPD CVVIVATLRG LKANSGHYDL
RPGMAIPDSI FSPDQAALVA GFENLKWHIK NVHKYGIPAV VAINQFPQDC EQELTALQDL
IHAFDPNVKV AISTAFAQGG EGTRDLAQYV VDACEKTTNF RPLYQKHQSL QEKLMSVCEA
GYGATNVEMS ELATKQLAHF EKLGFNELAV CIAKTPLSVT TDSSVKGAPV GFTVPIRELR
LCAGAGFVYA LSGSVMTMPG LPDKPAFMNL DLDEDGNIIG LS