FTCD_PIG
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 03-AUG-2022, entry version 129.
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 = (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; 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(+) = 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 PDBsum; 1QD1; -.
DR AlphaFoldDB; P53603; -.
DR SMR; P53603; -.
DR STRING; 9823.ENSSSCP00000022108; -.
DR PaxDb; P53603; -.
DR PeptideAtlas; P53603; -.
DR GeneID; 397517; -.
DR KEGG; ssc:397517; -.
DR CTD; 10841; -.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR InParanoid; P53603; -.
DR OrthoDB; 1063278at2759; -.
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 Proteomes; UP000314985; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
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:histidine catabolic process; IC:BHF-UCL.
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 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
