FTCD_DICDI
ID FTCD_DICDI Reviewed; 537 AA.
AC Q54JL3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000250|UniProtKB:P53603};
DE AltName: Full=Formiminotransferase-cyclodeaminase;
DE Short=FTCD;
DE AltName: Full=p60;
DE Includes:
DE RecName: Full=Glutamate formimidoyltransferase {ECO:0000250|UniProtKB:P53603};
DE EC=2.1.2.5 {ECO:0000250|UniProtKB:P53603};
DE AltName: Full=Glutamate formiminotransferase;
DE AltName: Full=Glutamate formyltransferase;
DE Includes:
DE RecName: Full=Formimidoyltetrahydrofolate cyclodeaminase {ECO:0000250|UniProtKB:P53603};
DE EC=4.3.1.4 {ECO:0000250|UniProtKB:P53603};
DE AltName: Full=Formiminotetrahydrofolate cyclodeaminase;
GN Name=ftcd; ORFNames=DDB_G0287977;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Folate-dependent enzyme, that displays both transferase and
CC deaminase activity. Serves to channel one-carbon units from
CC formiminoglutamate to the folate pool. {ECO:0000250|UniProtKB:O95954}.
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:0000250|UniProtKB:O95954};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099;
CC Evidence={ECO:0000250|UniProtKB:O95954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-
CC methenyltetrahydrofolate + NH4(+); Xref=Rhea:RHEA:22736,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57456; EC=4.3.1.4;
CC Evidence={ECO:0000250|UniProtKB:P53603};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737;
CC Evidence={ECO:0000250|UniProtKB:P53603};
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. {ECO:0000250|UniProtKB:O95954}.
CC -!- SUBUNIT: Homooctamer, including four polyglutamate binding sites. The
CC subunits are arranged as a tetramer of dimers, and form a planar ring-
CC shaped structure. {ECO:0000250|UniProtKB:O88618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9YH58}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O95954}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cyclodeaminase/cyclohydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC formiminotransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000107; EAL63414.1; -; Genomic_DNA.
DR RefSeq; XP_636918.1; XM_631826.1.
DR AlphaFoldDB; Q54JL3; -.
DR SMR; Q54JL3; -.
DR STRING; 44689.DDB0267047; -.
DR PaxDb; Q54JL3; -.
DR EnsemblProtists; EAL63414; EAL63414; DDB_G0287977.
DR GeneID; 8626393; -.
DR KEGG; ddi:DDB_G0287977; -.
DR dictyBase; DDB_G0287977; ftcd.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR HOGENOM; CLU_040037_1_0_1; -.
DR InParanoid; Q54JL3; -.
DR OMA; VGQPECV; -.
DR PhylomeDB; Q54JL3; -.
DR Reactome; R-DDI-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00555.
DR PRO; PR:Q54JL3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; IEA:UniProtKB-EC.
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 Gene3D; 1.20.120.680; -; 1.
DR Gene3D; 3.30.70.670; -; 1.
DR Gene3D; 3.30.990.10; -; 1.
DR InterPro; IPR007044; Cyclodeamin/CycHdrlase.
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 InterPro; IPR036178; Formintransfe-cycloase-like_sf.
DR Pfam; PF02971; FTCD; 1.
DR Pfam; PF04961; FTCD_C; 1.
DR Pfam; PF07837; FTCD_N; 1.
DR SMART; SM01221; FTCD; 1.
DR SMART; SM01222; FTCD_N; 1.
DR SUPFAM; SSF101262; SSF101262; 1.
DR SUPFAM; SSF55116; SSF55116; 2.
DR TIGRFAMs; TIGR02024; FtcD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Folate-binding; Golgi apparatus;
KW Histidine metabolism; Lyase; Multifunctional enzyme; Reference proteome;
KW Transferase.
FT CHAIN 1..537
FT /note="Formimidoyltransferase-cyclodeaminase"
FT /id="PRO_0000328198"
FT REGION 1..181
FT /note="Formiminotransferase N-subdomain"
FT /evidence="ECO:0000250"
FT REGION 182..326
FT /note="Formiminotransferase C-subdomain"
FT /evidence="ECO:0000250"
FT REGION 327..335
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 336..537
FT /note="Cyclodeaminase/cyclohydrolase"
FT /evidence="ECO:0000250"
FT ACT_SITE 82
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /note="For cyclodeaminase activity"
FT /evidence="ECO:0000250"
FT BINDING 163..172
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 59257 MW; B23C491EBFC04125 CRC64;
MNKLVECVPN FSEGRDQTII DAISKAIRDT AGCTLLDVDP GKSTNRTVYT FVGCPDSIVN
GAINATKVAF KLIDMTKHHG EHPRMGALDV CPFVPVRNVT MEECVNCSKE FGKRISEEIG
VPIFLYEEAS TQSYRKQLKQ IRQGEYEGLE EKLKEEKWKP DFGPAKFIPS YGASVTGARS
FLIAYNVNIL GTKEQAHRIA LNVREAGRGD NEPGRLKFLK GIGWFVDEYN LAQVSMNLDN
YRETGVHTVF EECSKDAREL NLGVAGSEIV GLVPLEAILM AADYYIAKEN LFIIDEALKV
RLAIERLGLS SCSFFDPKKR IIDYMVQEDL KVTQPLASMS VRGFVELLGS RTPAPGGGSA
SALIAAMGAG LGAMTGWMTF GKKKFEALDS IMRELLPPLD KAMRDLIPYI DADTNAFNDY
IKAMGTPKGP QRDIAIDKAL KQAINIPLST MKISNTCWGP LLKMAQYGNL ASKSDLEVGC
KSLETGIWGA HRNVSINLLD CKDAQFVEST TKEANEILKN AQESLQKVLE ILSNRKE
