GLFT_PICTO
ID GLFT_PICTO Reviewed; 301 AA.
AC Q6KZM5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=PTO1242;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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=0.4 uM for 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=0.7 uM for 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=34 uM for Glu (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC Note=kcat is 1.16 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; AE017261; AAT43827.1; -; Genomic_DNA.
DR RefSeq; WP_011178043.1; NC_005877.1.
DR AlphaFoldDB; Q6KZM5; -.
DR SMR; Q6KZM5; -.
DR STRING; 263820.PTO1242; -.
DR EnsemblBacteria; AAT43827; AAT43827; PTO1242.
DR GeneID; 2844665; -.
DR KEGG; pto:PTO1242; -.
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; UP000000438; 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..301
FT /note="Glutamate formimidoyltransferase"
FT /id="PRO_0000430019"
FT ACT_SITE 86
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 168..176
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255"
SQ SEQUENCE 301 AA; 34042 MW; 0818B6088AEC299D CRC64;
MPDKEVKIVE AVPNFSEGRD ISKIEKIIDS IKNIEGVKIL DLNVDPQHNR SVITFTCGIE
RIIEAGISMI KTAASLIDME KHSGLHPRFG ATDVFPIIPI TASMDDCIIA SRNLGRLVGS
ELNIPVYMYS ESAMVPERRN LENIRNKNVQ YEELKELIKT DKYRPDFGPD SLGSAGAVII
GARPALIAYN IYISTDDIKI GRRIASALRG RDGGLNTLKT LAFYIEARKM VQISMNITDY
KKTSIYKIFE LLSIECRRYN VYPVESELIG LMPMDALIDV FNYYMKSNIT RDKILEYKIF
T
