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Database: UniProt
Entry: Q1PUK7_KUEST
LinkDB: Q1PUK7_KUEST
Original site: Q1PUK7_KUEST 
ID   Q1PUK7_KUEST            Unreviewed;       587 AA.
AC   Q1PUK7;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000256|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000256|HAMAP-Rule:MF_01543};
GN   Name=ftsH {ECO:0000313|EMBL:CAJ70914.1};
GN   Synonyms=fhs {ECO:0000256|HAMAP-Rule:MF_01543,
GN   ECO:0000313|EMBL:QII13314.1}, ftsH_6 {ECO:0000313|EMBL:SOH05655.1};
GN   ORFNames=KsCSTR_39350 {ECO:0000313|EMBL:QII13314.1}, KSMBR1_3178
GN   {ECO:0000313|EMBL:SOH05655.1}, kustb0169
GN   {ECO:0000313|EMBL:CAJ70914.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ70914.1};
RN   [1] {ECO:0000313|EMBL:CAJ70914.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16598256; DOI=10.1038/nature04647;
RA   Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA   Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA   Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA   Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA   vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA   Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA   Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA   LePaslier D.;
RT   "Deciphering the evolution and metabolism of an anammox bacterium from a
RT   community genome.";
RL   Nature 440:790-794(2006).
RN   [2] {ECO:0000313|EMBL:CAJ70914.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SOH05655.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH05655.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QII13314.1, ECO:0000313|Proteomes:UP000501926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSTR1 {ECO:0000313|EMBL:QII13314.1,
RC   ECO:0000313|Proteomes:UP000501926};
RA   Ding C., Adrian L.;
RT   "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT   Kuenenia stuttgartiensis genomes.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01543}.
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DR   EMBL; CT573074; CAJ70914.1; -; Genomic_DNA.
DR   EMBL; CP049055; QII13314.1; -; Genomic_DNA.
DR   EMBL; LT934425; SOH05655.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1PUK7; -.
DR   KEGG; kst:KSMBR1_3178; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR   Proteomes; UP000501926; 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 {ECO:0000256|HAMAP-Rule:MF_01543};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01543, ECO:0000313|EMBL:CAJ70914.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01543}; Reference proteome {ECO:0000313|Proteomes:UP000221734}.
FT   BINDING         74..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   587 AA;  63482 MW;  F29DDAAC7E764847 CRC64;
     MSLDPTKFAD WQIAEEAEKG MKTVYELADK LGLAKEELLP HGHYVAKVDY KKILKRYEGK
     PDGKFVDVTA ITPTPLGEGK STTTIGLVQG LGKRGKNVIG TIRQPSGGPT MNIKGSAAGG
     GLSQCIPLTP FSLGLTGDIN AIMNAHNLAM VALTSRMQHE FNYDDATLAK KNLRRLNIDP
     HRVEMKWIID FCAQSLRQIV IGLGGKMDGF MMESGFAIAV SSEIMAILSV AKDLKDMRER
     MGKIVVAYDK SGKPVTTADL EVDGAMTAWM VEALNPNLMQ TIEGQPVFVH AGPFANIAIG
     QSSIVADRIA LKLGDYVVTE SGFGADIGFE KFWNLKCRFS GSKPNAAVLV ATVRALKCHG
     GAPVPVPGHP LDPCYKEENV GWVEKGTENL THLINVVKKA GINPVVCINA FYTDTEPEIN
     AVRRLAERAG ARVALSKHWL KGGDGAVELA DAVIDACNEP NDFKFLYELS TPLRTRIELI
     AEQVYGADGV DYSPDALAKV KAMEADPETS KLGTCMVKTH LSLTDNPNIK GAPKNWRLSI
     RDILTFKGAG FVVPIAGNIK LMPGTCSDPA YRRVDVDVET GKVKGLF
//
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