FTCD_CHICK
ID FTCD_CHICK Reviewed; 541 AA.
AC Q9YH58;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000305|PubMed:9677386};
DE AltName: Full=Formiminotransferase-cyclodeaminase;
DE Short=FTCD;
DE AltName: Full=p60;
DE Includes:
DE RecName: Full=Glutamate formimidoyltransferase {ECO:0000305|PubMed:9677386};
DE EC=2.1.2.5 {ECO:0000269|PubMed:9677386};
DE AltName: Full=Glutamate formiminotransferase;
DE AltName: Full=Glutamate formyltransferase;
DE Includes:
DE RecName: Full=Formimidoyltetrahydrofolate cyclodeaminase {ECO:0000305|PubMed:9677386};
DE EC=4.3.1.4 {ECO:0000269|PubMed:9677386};
DE AltName: Full=Formiminotetrahydrofolate cyclodeaminase;
GN Name=FTCD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9677386; DOI=10.1074/jbc.273.31.19602;
RA Hennig D., Scales S.J., Moreau A., Murley L.L., De Mey J., Kreis T.E.;
RT "A formiminotransferase cyclodeaminase isoform is localized to the Golgi
RT complex and can mediate interaction of trans-Golgi network-derived vesicles
RT with microtubules.";
RL J. Biol. Chem. 273:19602-19611(1998).
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:9677386}.
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:9677386};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099;
CC Evidence={ECO:0000305|PubMed:9677386};
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:9677386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737;
CC Evidence={ECO:0000305|PubMed:9677386};
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:9677386}.
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 {ECO:0000269|PubMed:9677386}.
CC Golgi apparatus {ECO:0000269|PubMed:9677386}. Cytoplasm, cytoskeleton,
CC microtubule 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; AJ224473; CAA11966.1; -; mRNA.
DR RefSeq; NP_990234.1; NM_204903.1.
DR AlphaFoldDB; Q9YH58; -.
DR SMR; Q9YH58; -.
DR STRING; 9031.ENSGALP00000009880; -.
DR PaxDb; Q9YH58; -.
DR GeneID; 395726; -.
DR KEGG; gga:395726; -.
DR CTD; 10841; -.
DR VEuPathDB; HostDB:geneid_395726; -.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR InParanoid; Q9YH58; -.
DR OrthoDB; 1063278at2759; -.
DR PhylomeDB; Q9YH58; -.
DR BRENDA; 2.1.2.5; 1306.
DR BRENDA; 4.3.1.4; 1306.
DR UniPathway; UPA00379; UER00555.
DR PRO; PR:Q9YH58; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; IDA:UniProtKB.
DR GO; GO:0030409; F:glutamate formimidoyltransferase activity; IDA:UniProtKB.
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 Cytoplasm; Cytoskeleton; Folate-binding; Golgi apparatus;
KW Histidine metabolism; Lyase; Multifunctional enzyme; Reference proteome;
KW Transferase.
FT CHAIN 1..541
FT /note="Formimidoyltransferase-cyclodeaminase"
FT /id="PRO_0000285576"
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:0000250"
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"
SQ SEQUENCE 541 AA; 59154 MW; A37BEF9654D46470 CRC64;
MAKLVECVPN FSEGCNKEVI EALGRAISQT PGCTLLDVDA GASTNRTVYT FVGTPEAVVE
GALSAARMAW ELIDMSRHKG EHPRMGALDV CPFVPVMNIS MEECVICAHV FGQRLSEELG
VPVYLYGEAA RQESRRTLPA IRAGEYEALP KKLEKPEWVP DFGPPAFVPQ WGATVTGART
FLIAYNINLL CTKELAHRIA LNIREQGRGA DQPGSLKKVQ GIGWYLEEEN IAQVSTNLLD
FETTPLHAVY EEVCYNAEAL KLPVVGSQLV GLVPKKAMLD AAEFYIKKEK LFILEEEHKI
KLVVSRLGLD SLSPFNPRER IIEYLVQAGQ EDKGLVTKPL GAFVRAVGGR SAAPGGGSVA
ATAASLGAAL GCMVGLMSYG KRQFEQLDSI MRNVIPPLHQ AMDELVAMVD ADSRAFSSYM
EAMKLPKSTP EERERRVVAM QQGLKTAVEV PCTLAVKVNN LWSSLKMLAH HGNLACKSDL
QVGAKMLEAA VFGAYFNVMI NLKDITDEKF KTETSQMVTR LLEEAKQGSA LVLALLEKRE
A
