GLFT_STRP1
ID GLFT_STRP1 Reviewed; 299 AA.
AC Q99XR4; Q48W85;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=M5005_Spy1772, SPy_2083;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
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=4.8 uM for 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=5.4 uM for 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC KM=1030 uM for Glu (at pH 7.3 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20952389};
CC Note=kcat is 0.13 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; AE004092; AAK34736.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52390.1; -; Genomic_DNA.
DR RefSeq; NP_270015.1; NC_002737.2.
DR AlphaFoldDB; Q99XR4; -.
DR SMR; Q99XR4; -.
DR STRING; 1314.HKU360_01885; -.
DR PaxDb; Q99XR4; -.
DR PRIDE; Q99XR4; -.
DR EnsemblBacteria; AAK34736; AAK34736; SPy_2083.
DR KEGG; spy:SPy_2083; -.
DR KEGG; spz:M5005_Spy1772; -.
DR PATRIC; fig|160490.10.peg.1805; -.
DR HOGENOM; CLU_040037_0_0_9; -.
DR OMA; DEDHNRL; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000000750; 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..299
FT /note="Glutamate formimidoyltransferase"
FT /id="PRO_0000430017"
FT ACT_SITE 82
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 163..172
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255"
SQ SEQUENCE 299 AA; 33305 MW; 58B290889C799895 CRC64;
MAKIVECIPN FSEGQNQAVI DGLVATAKSI PGVTLLDYSS DASHNRSVFT LVGDDQSIQE
AAFQLVKYAS ENIDMTKHHG EHPRMGATDV CPFVPIKDIT TQECVEISKQ VAERINRELG
IPIFLYEDSA TRPERQNLAK VRKGQFEGMP EKLLEEDWAP DYGDRKIHPT AGVTAVGARM
PLVAFNVNLD TDNIDIAHKI AKIIRGSGGG YKYCKAIGVM LEDRHIAQVS MNMVNFEKCS
LYRTFETIKF EARRYGVNVI GSEVIGLAPA KALIDVAEYY LQVEDFDYHK QILENHLLG
