FTHS_SHESR
ID FTHS_SHESR Reviewed; 569 AA.
AC Q0HR05;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Shewmr7_3469;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI44450.1; -; Genomic_DNA.
DR RefSeq; WP_011627283.1; NC_008322.1.
DR AlphaFoldDB; Q0HR05; -.
DR SMR; Q0HR05; -.
DR PRIDE; Q0HR05; -.
DR EnsemblBacteria; ABI44450; ABI44450; Shewmr7_3469.
DR KEGG; shm:Shewmr7_3469; -.
DR HOGENOM; CLU_003601_3_3_6; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
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; -; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT CHAIN 1..569
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300540"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 569 AA; 59585 MW; FD9E42B843914AB0 CRC64;
MLTDMDISRR ADLKDIAALG AEFGLLPDEM QLFGKTKAKV DLRVQQRLAE QQGKLIIVTA
VTPTPHGEGK TVTTIGLTQS LKALGNKVCA CIRQPSMGPV FGVKGGAAGG GYAQVVPMQE
LNLHLTGDIH AVSSAHNLGA AAIASRLYHE TRLGKAEFEL QSGQNYLDIA PNGIRWHRVV
DHNDRCLREI EVGLGENNGP AYTSGFDITA ASELMAILAL SRNLADMRAR IGKLVLAVNR
QGAAISAEDL GVAGAMTALM ADAVKPTLMQ TLNGAPCLIH AGPFANIAHG NSSVIADDIA
LKLADFVVTE GGFGSDMGFE KFCNIKARQS GLAPSTAVLV TTLKALKANS GLTSDADINA
PDQARLEAGF ANLNWHINNV ARYGIPVVVA INRFATDTDA ELNWLIEAVS GTAAFGCELS
ETFSQGEAGA LALAQTVMRA CEQPSEFTLL YPDDMALEAK LSTLAEVGYG AAGVSLSEAA
KLQLQELSAL GYAHLPVCMA KTPLSISHDP QLKGVPQGFI VPVRELVLNA GAGFITALVG
NVMTMPGLGL VPGYLKIDIG ADGEITGLG
