ID H3NMG2_9FIRM Unreviewed; 547 AA.
AC H3NMG2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN ORFNames=HMPREF9709_00523 {ECO:0000313|EMBL:EHR35048.1};
OS Helcococcus kunzii ATCC 51366.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Helcococcus.
OX NCBI_TaxID=883114 {ECO:0000313|EMBL:EHR35048.1, ECO:0000313|Proteomes:UP000004191};
RN [1] {ECO:0000313|EMBL:EHR35048.1, ECO:0000313|Proteomes:UP000004191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51366 {ECO:0000313|EMBL:EHR35048.1,
RC ECO:0000313|Proteomes:UP000004191};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Helcococcus kunzii ATCC 51366.";
RL Submitted (JAN-2012) 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|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000256|HAMAP-Rule:MF_01543}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHR35048.1}.
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DR EMBL; AGEI01000014; EHR35048.1; -; Genomic_DNA.
DR RefSeq; WP_005397698.1; NZ_JH601088.1.
DR AlphaFoldDB; H3NMG2; -.
DR STRING; 883114.HMPREF9709_00523; -.
DR PATRIC; fig|883114.3.peg.517; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OrthoDB; 9761733at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000004191; Unassembled WGS sequence.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF01268; FTHFS; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01543};
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:UP000004191}.
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 547 AA; 59882 MW; D2EB5A26FB7CBFE4 CRC64;
MKTDYEISLE AKKENIETIA SKMGVEKEDL VKYGNYKAKI KFDKFDNLSK NLILVTSINP
TSTGEGKSTV TVGLSDGLNK IGKKSVVALR EPSFGPVLGR KGGATGGGYA QVVPMEEINL
HFNGDLHAIT SAHNAIMSLI NNHIFQGNEL GFERVEFNYV LDMNERALRS IKINAGKKSE
RDSYFEITVA SEIMAILCLA ENLDDLKQKI ANMLIGFNKA NEPIYVKDLK IEGVVTAILR
DALNPNLVQS LENNPAIIHG GPFANIAHGC NSVIATKTAL KYGEYVVTEA GFGADLGAEK
FIDIKCRKSG LRPKAAVIVA TIKALKLHGG VKESDLNIEN LGALKTGLEN IEKHIENMNK
FNLPVIIALN KFVTDTDAEI QLIENWAKEI GVEFSLTEVW AKGGEGAIDL AEKVVNIVEN
NKQELKFIYE DEDSIEDKIN KVAKEIYGAS SVNFTDESLI KLGRINLLGY NNLPICIAKT
PNSLSDNPKL IGRPRDFEIT VTDMNIRSGA GFIVVYLNKV MTMPGLPKVP NALAIDVNEE
GNIVNLF
//