GLFT_THEAC
ID GLFT_THEAC Reviewed; 303 AA.
AC Q9HI69;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glutamate formimidoyltransferase;
DE EC=2.1.2.5;
DE AltName: Full=5-formyltetrahydrofolate cyclo-ligase;
DE EC=6.3.3.2;
DE AltName: Full=Glutamate formiminotransferase;
DE AltName: Full=Glutamate formyltransferase;
GN OrderedLocusNames=Ta1476;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=20952389; DOI=10.1074/jbc.m110.190504;
RA Jeanguenin L., Lara-Nunez A., Pribat A., Mageroy M.H., Gregory J.F. III,
RA Rice K.C., de Crecy-Lagard V., Hanson A.D.;
RT "Moonlighting glutamate formiminotransferases can functionally replace 5-
RT formyltetrahydrofolate cycloligase.";
RL J. Biol. Chem. 285:41557-41566(2010).
CC -!- FUNCTION: Catalyzes the transfer of the formyl group from N-
CC formylglutamate to tetrahydrofolate (THF) to yield 5-
CC formyltetrahydrofolate (5-CHO-THF) and glutamate (Glu). The
CC triglutamate form of 5-CHO-THF (5-CHO-THF-Glu3) can also be used as
CC substrate. It can also catalyzes the transfer of the formimino group
CC from N-formiminoglutamate to tetrahydrofolate (THF) to yield 5-
CC formiminotetrahydrofolate (5-NH=CH-THF) and glutamate (Glu). It can
CC replace YgfA to catalyzes the irreversible ATP-dependent transformation
CC of 5-CHO-THF to form 5,10-methenyltetrahydrofolate (5,10-CH=THF).
CC {ECO:0000269|PubMed:20952389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + L-glutamate = (6S)-
CC 5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-glutamate;
CC Xref=Rhea:RHEA:23240, ChEBI:CHEBI:15378, ChEBI:CHEBI:17684,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57457; EC=2.1.2.5;
CC Evidence={ECO:0000269|PubMed:20952389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-
CC tetrahydrofolate + N-formimidoyl-L-glutamate; Xref=Rhea:RHEA:15097,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57456,
CC ChEBI:CHEBI:58928; EC=2.1.2.5;
CC Evidence={ECO:0000269|PubMed:20952389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = 5,10-
CC methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC Evidence={ECO:0000269|PubMed:20952389};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=3.8 uM for 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=113 uM for Glu (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC Note=kcat is 0.27 sec(-1) for formyltransferase with 5-CHO-THF or 5-
CC CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).;
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase
CC route): step 1/1.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formiminotransferase family. {ECO:0000305}.
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DR EMBL; AL445067; CAC12594.1; -; Genomic_DNA.
DR RefSeq; WP_010901876.1; NC_002578.1.
DR AlphaFoldDB; Q9HI69; -.
DR SMR; Q9HI69; -.
DR STRING; 273075.Ta1476; -.
DR MoonProt; Q9HI69; -.
DR EnsemblBacteria; CAC12594; CAC12594; CAC12594.
DR GeneID; 1456928; -.
DR KEGG; tac:Ta1476; -.
DR eggNOG; arCOG05394; Archaea.
DR HOGENOM; CLU_040037_0_0_2; -.
DR OMA; DEDHNRL; -.
DR OrthoDB; 67788at2157; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0030409; F:glutamate formimidoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.670; -; 1.
DR Gene3D; 3.30.990.10; -; 1.
DR InterPro; IPR013802; Formiminotransferase_C.
DR InterPro; IPR037070; Formiminotransferase_C_sf.
DR InterPro; IPR004227; Formiminotransferase_cat.
DR InterPro; IPR012886; Formiminotransferase_N.
DR InterPro; IPR037064; Formiminotransferase_N_sf.
DR InterPro; IPR022384; FormiminoTrfase_cat_dom_sf.
DR Pfam; PF02971; FTCD; 1.
DR Pfam; PF07837; FTCD_N; 1.
DR SMART; SM01221; FTCD; 1.
DR SMART; SM01222; FTCD_N; 1.
DR SUPFAM; SSF55116; SSF55116; 2.
DR TIGRFAMs; TIGR02024; FtcD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Folate-binding; Histidine metabolism; Ligase;
KW Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Glutamate formimidoyltransferase"
FT /id="PRO_0000430018"
FT ACT_SITE 81
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 164..172
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255"
SQ SEQUENCE 303 AA; 33792 MW; AB78C109F403A30A CRC64;
MSLVECVPNF SEGRDRDRVN RIRDAIASVD TVKILDVEMD PNHNRSVITF VCDSSKAVDA
AFAGIKAAAE IIDMDAHRGE HPRFGAADVI PFVPLQDTKM ETCVRLARDL GKRVGEELGI
PVYLYAEAAQ RPDRSDLAAI RNKNFQYEQL KEAIKEEKWK PDFGPSVVGK AGASIIGARD
FLIAYNVNLN TSNMEIGKKI ASAIRAKDGG LTFVKSLAFF LKDKNMVQIS MNLTNYRKTP
IYRAYELVRL EAARYGVLPV ESEIVGLVPE QALIDVAKYY LQLNGFDEGN ILERKMEKAA
NME
