ID   FTCD_PIG                Reviewed;         541 AA.
AC   P53603;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 140.
DE   RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000305|PubMed:7901203};
DE   AltName: Full=Formiminotransferase-cyclodeaminase;
DE            Short=FTCD;
DE   Includes:
DE     RecName: Full=Glutamate formimidoyltransferase {ECO:0000305|PubMed:7901203};
DE              EC=2.1.2.5 {ECO:0000269|PubMed:7901203};
DE     AltName: Full=Glutamate formiminotransferase;
DE     AltName: Full=Glutamate formyltransferase;
DE   Includes:
DE     RecName: Full=Formimidoyltetrahydrofolate cyclodeaminase {ECO:0000305|PubMed:7901203};
DE              EC=4.3.1.4 {ECO:0000269|PubMed:7901203};
DE     AltName: Full=Formiminotetrahydrofolate cyclodeaminase;
GN   Name=FTCD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 392-410 AND 424-453,
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=Yucatan; TISSUE=Liver;
RX   PubMed=7901203; DOI=10.1016/s0021-9258(18)41601-8;
RA   Murley L.L., Mejia N.R., Mackenzie R.E.;
RT   "The nucleotide sequence of porcine formiminotransferase cyclodeaminase.
RT   Expression and purification from Escherichia coli.";
RL   J. Biol. Chem. 268:22820-22824(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-326.
RX   PubMed=10673422; DOI=10.1016/s0969-2126(00)00078-2;
RA   Kohls D., Sulea T., Purisima E.O., MacKenzie R.E., Vrielink A.;
RT   "The crystal structure of the formiminotransferase domain of
RT   formiminotransferase-cyclodeaminase: implications for substrate channeling
RT   in a bifunctional enzyme.";
RL   Structure 8:35-46(2000).
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:0000269|PubMed:7901203}.
CC   -!- FUNCTION: Binds and promotes bundling of vimentin filaments originating
CC       from the Golgi. {ECO:0000250|UniProtKB:O88618}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-formimidoyltetrahydrofolate + L-glutamate = N-formimidoyl-L-
CC         glutamate + (6S)-5,6,7,8-tetrahydrofolate; Xref=Rhea:RHEA:15097,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57456,
CC         ChEBI:CHEBI:58928; EC=2.1.2.5; Evidence={ECO:0000269|PubMed:7901203};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099;
CC         Evidence={ECO:0000305|PubMed:7901203};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-formimidoyltetrahydrofolate + 2 H(+) = (6R)-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; Evidence={ECO:0000269|PubMed:7901203};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737;
CC         Evidence={ECO:0000305|PubMed:7901203};
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:0000305|PubMed:7901203}.
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}. Note=More abundantly located around the
CC       mother centriole. {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; L16507; AAA31034.1; -; mRNA.
DR   PIR; A48717; A48717.
DR   RefSeq; NP_999440.1; NM_214275.1.
DR   PDB; 1QD1; X-ray; 1.70 A; A/B=2-326.
DR   AlphaFoldDB; P53603; -.
DR   SMR; P53603; -.
DR   FunCoup; P53603; 284.
DR   STRING; 9823.ENSSSCP00000022108; -.
DR   PaxDb; 9823-ENSSSCP00000022108; -.
DR   PeptideAtlas; P53603; -.
DR   GeneID; 397517; -.
DR   KEGG; ssc:397517; -.
DR   CTD; 10841; -.
DR   eggNOG; ENOG502QQBY; Eukaryota.
DR   InParanoid; P53603; -.
DR   OrthoDB; 48036at2759; -.
DR   BRENDA; 2.1.2.5; 6170.
DR   BRENDA; 4.3.1.4; 6170.
DR   SABIO-RK; P53603; -.
DR   UniPathway; UPA00379; UER00555.
DR   EvolutionaryTrace; P53603; -.
DR   Proteomes; UP000008227; Unplaced.
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; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005542; F:folic acid binding; IEA:InterPro.
DR   GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; IDA:BHF-UCL.
DR   GO; GO:0030409; F:glutamate formimidoyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0006548; P:L-histidine catabolic process; IC:BHF-UCL.
DR   FunFam; 1.20.120.680:FF:000001; Formimidoyltransferase cyclodeaminase; 1.
DR   FunFam; 3.30.70.670:FF:000001; Formimidoyltransferase cyclodeaminase; 1.
DR   FunFam; 3.30.990.10:FF:000001; Formimidoyltransferase cyclodeaminase; 1.
DR   Gene3D; 1.20.120.680; Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle; 1.
DR   Gene3D; 3.30.70.670; Formiminotransferase, C-terminal subdomain; 1.
DR   Gene3D; 3.30.990.10; Formiminotransferase, N-terminal subdomain; 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   InterPro; IPR051623; FTCD.
DR   NCBIfam; TIGR02024; FtcD; 1.
DR   PANTHER; PTHR12234:SF0; FORMIMIDOYLTRANSFERASE-CYCLODEAMINASE; 1.
DR   PANTHER; PTHR12234; FORMIMINOTRANSFERASE-CYCLODEAMINASE; 1.
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; SSF55116; Formiminotransferase domain of formiminotransferase-cyclodeaminase; 2.
DR   SUPFAM; SSF101262; Methenyltetrahydrofolate cyclohydrolase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Folate-binding; Golgi apparatus; Histidine metabolism; Lyase;
KW   Multifunctional enzyme; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..541
FT                   /note="Formimidoyltransferase-cyclodeaminase"
FT                   /id="PRO_0000087361"
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..334
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          335..541
FT                   /note="Cyclodeaminase/cyclohydrolase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        82
FT                   /note="For formimidoyltransferase activity"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        412
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"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88618"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           17..28
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   TURN            42..45
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           55..72
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          85..98
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           101..119
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           138..142
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           145..152
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          183..191
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           193..203
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          219..226
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   TURN            227..230
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          231..239
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   TURN            241..243
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           246..259
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          264..271
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           275..289
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           296..307
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:1QD1"
FT   HELIX           322..325
FT                   /evidence="ECO:0007829|PDB:1QD1"
SQ   SEQUENCE   541 AA;  58930 MW;  D52974A9EE088DDF CRC64;
     MSQLVECVPN FSEGKNQEVI DAISRAVAQT PGCVLLDVDS GPSTNRTVYT FVGRPEDVVE
     GALNAARAAY QLIDMSRHHG EHPRMGALDV CPFIPVRGVT MDECVRCAQA FGQRLAEELG
     VPVYLYGEAA RTAGRQSLPA LRAGEYEALP EKLKQAEWAP DFGPSAFVPS WGATVAGARK
     FLLAFNINLL STREQAHRIA LDLREQGRGK DQPGRLKKVQ AIGWYLDEKN LAQVSTNLLD
     FEVTGLHTVF EETCREAQEL SLPVVGSQLV GLVPLKALLD AAAFYCEKEN LFLLQDEHRI
     RLVVNRLGLD SLAPFKPKER IIEYLVPEAG PEQSLLHKPL RTFVREVGSR SAAPGAGSVA
     AATAAMGAAL ASMVGLMTYG RRQFEHLDAT MRRLIPPFHA ASAKLTSLVD ADARAFEAYL
     KAMKLPKDTP EDKDRRAAAL QEGLRQAVAV PLALAETVAS LWPALQELAL CGNLACRSDL
     QVAAKALETG VFGAYFNVLI NLKDVTDDAF KAQVRQRISS LLQEAKTQAA LVLDRLEARQ
     A
//