FTCD_RAT
ID FTCD_RAT Reviewed; 541 AA.
AC O88618; Q5BKB7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000305|PubMed:9677387};
DE AltName: Full=58 kDa microtubule-binding protein;
DE AltName: Full=Formiminotransferase-cyclodeaminase;
DE Short=FTCD;
DE Includes:
DE RecName: Full=Glutamate formimidoyltransferase {ECO:0000305|PubMed:9677387};
DE EC=2.1.2.5 {ECO:0000269|PubMed:9677387};
DE AltName: Full=Glutamate formiminotransferase;
DE AltName: Full=Glutamate formyltransferase;
DE Includes:
DE RecName: Full=Formimidoyltetrahydrofolate cyclodeaminase {ECO:0000305|PubMed:9677387};
DE EC=4.3.1.4 {ECO:0000269|PubMed:9677387};
DE AltName: Full=Formiminotetrahydrofolate cyclodeaminase;
GN Name=Ftcd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 257.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Gao Y.-S., Sztul E.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-48; 88-179 AND 223-285.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9837973; DOI=10.1074/jbc.273.50.33825;
RA Gao Y.-S., Alvarez C., Nelson D.S., Sztul E.;
RT "Molecular cloning, characterization, and dynamics of rat
RT formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein.";
RL J. Biol. Chem. 273:33825-33834(1998).
RN [4]
RP PROTEIN SEQUENCE OF 48-65; 115-136; 156-165; 257-268; 291-299; 307-318;
RP 321-341 AND 394-413, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9677387; DOI=10.1074/jbc.273.31.19612;
RA Bashour A.-M., Bloom G.S.;
RT "58K, a microtubule-binding Golgi protein, is a formiminotransferase
RT cyclodeaminase.";
RL J. Biol. Chem. 273:19612-19617(1998).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12160147; DOI=10.1078/0171-9335-00260;
RA Gao Y.S., Vrielink A., MacKenzie R., Sztul E.;
RT "A novel type of regulation of the vimentin intermediate filament
RT cytoskeleton by a Golgi protein.";
RL Eur. J. Cell Biol. 81:391-401(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), SUBUNIT, AND ACTIVE SITE FOR
RP CYCLODEAMINASE ACTIVITY.
RX PubMed=15272307; DOI=10.1038/sj.emboj.7600327;
RA Mao Y., Vyas N.K., Vyas M.N., Chen D.H., Ludtke S.J., Chiu W.,
RA Quiocho F.A.;
RT "Structure of the bifunctional and Golgi-associated formiminotransferase
RT cyclodeaminase octamer.";
RL EMBO J. 23:2963-2971(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), AND SUBUNIT.
RX PubMed=17470791; DOI=10.1073/pnas.0701204104;
RA Poon B.K., Chen X., Lu M., Vyas N.K., Quiocho F.A., Wang Q., Ma J.;
RT "Normal mode refinement of anisotropic thermal parameters for a
RT supramolecular complex at 3.42-A crystallographic resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7869-7874(2007).
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:9677387}.
CC -!- FUNCTION: Binds and promotes bundling of vimentin filaments originating
CC from the Golgi. {ECO:0000269|PubMed:12160147}.
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:9677387};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099;
CC Evidence={ECO:0000305|PubMed:9677387};
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:9677387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737;
CC Evidence={ECO:0000305|PubMed:9677387};
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:9677387}.
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:0000269|PubMed:15272307,
CC ECO:0000269|PubMed:17470791}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus
CC {ECO:0000269|PubMed:12160147, ECO:0000269|PubMed:9677387}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O95954}. Note=More abundantly located around the
CC mother centriole. {ECO:0000250|UniProtKB:O95954}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in liver (at protein level).
CC {ECO:0000269|PubMed:9677387}.
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; AF079233; AAC28849.3; -; mRNA.
DR EMBL; BC091134; AAH91134.1; -; mRNA.
DR RefSeq; NP_446019.1; NM_053567.1.
DR PDB; 1TT9; X-ray; 3.42 A; A/B/C/D=1-541.
DR PDB; 2PFD; X-ray; 3.42 A; A/B/C/D=1-541.
DR PDBsum; 1TT9; -.
DR PDBsum; 2PFD; -.
DR AlphaFoldDB; O88618; -.
DR SMR; O88618; -.
DR STRING; 10116.ENSRNOP00000001699; -.
DR iPTMnet; O88618; -.
DR PhosphoSitePlus; O88618; -.
DR PaxDb; O88618; -.
DR PRIDE; O88618; -.
DR Ensembl; ENSRNOT00000001699; ENSRNOP00000001699; ENSRNOG00000001261.
DR GeneID; 89833; -.
DR KEGG; rno:89833; -.
DR UCSC; RGD:70915; rat.
DR CTD; 10841; -.
DR RGD; 70915; Ftcd.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR GeneTree; ENSGT00390000005581; -.
DR HOGENOM; CLU_040037_1_0_1; -.
DR InParanoid; O88618; -.
DR OMA; VGQPECV; -.
DR OrthoDB; 1063278at2759; -.
DR PhylomeDB; O88618; -.
DR TreeFam; TF333892; -.
DR BRENDA; 2.1.2.5; 5301.
DR BRENDA; 4.3.1.4; 5301.
DR Reactome; R-RNO-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00555.
DR EvolutionaryTrace; O88618; -.
DR PRO; PR:O88618; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001261; Expressed in liver and 8 other tissues.
DR Genevisible; O88618; RN.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:RGD.
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:0019215; F:intermediate filament binding; TAS:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:RGD.
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_0000087362"
FT REGION 1..181
FT /note="Formiminotransferase N-subdomain"
FT REGION 182..326
FT /note="Formiminotransferase C-subdomain"
FT REGION 327..334
FT /note="Linker"
FT REGION 335..541
FT /note="Cyclodeaminase/cyclohydrolase"
FT ACT_SITE 82
FT /note="For formimidoyltransferase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="For cyclodeaminase activity"
FT /evidence="ECO:0000305|PubMed:15272307"
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:0007744|PubMed:22673903"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 357..377
FT /evidence="ECO:0007829|PDB:2PFD"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 388..406
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 408..423
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:2PFD"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 436..468
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 477..502
FT /evidence="ECO:0007829|PDB:2PFD"
FT HELIX 508..539
FT /evidence="ECO:0007829|PDB:2PFD"
SQ SEQUENCE 541 AA; 58914 MW; 76D806CE23478D92 CRC64;
MSQLVECVPN FSEGNNQEVI DAISQAISQT PGCVLLDVDA GPSTNRTVYT FVGQPECVVE
GALSAARTAS QLIDMRKHKG EHPRMGALDV CPFIPVRGVS MDECVLCAKA FGQRLAEELN
VPVYLYGEAA QMPSRQTLPA IRAGEYEALP EKLKQAEWVP DFGPSSFVPS WGATVTGARK
FLIAFNINLL STKEQAHRIA LNLREQGRGK DQPGRLKKVQ GIGWYLEEKN LAQVSTNLLD
FEVTALHTVY EEARREAQEL NLPVVGSQLV GLVPLKALLD AAAFYCDKEK LFVLEEEHRI
RLVVNRLGLD SLAPFDPKER IIEYLVPDSG PEQSLLDASL RAFVREVGAR SAAPGGGSVA
AAVAALGAAL ASMVGQMTYG RRQFDHLDST MRRLIPPFHA ASAQLTSLVD ADARAFAACL
GAIKLPKNTP EERDRRTCAL QEGLRQAVAV PLKLAETVSQ LWPALQELAQ CGNLSCLSDL
QVAAKALETG VFGAYFNVLI NLKDMTDDVF KEKTRHRISS LLQEAKTQAA LVLGSLEARK
E
