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Database: UniProt
Entry: F7DDZ6_ORNAN
LinkDB: F7DDZ6_ORNAN
Original site: F7DDZ6_ORNAN 
ID   F7DDZ6_ORNAN            Unreviewed;       541 AA.
AC   F7DDZ6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Formimidoyltransferase-cyclodeaminase {ECO:0000256|ARBA:ARBA00017787};
DE            EC=2.1.2.5 {ECO:0000256|ARBA:ARBA00012252};
DE            EC=4.3.1.4 {ECO:0000256|ARBA:ARBA00012998};
DE   AltName: Full=Formiminotransferase-cyclodeaminase {ECO:0000256|ARBA:ARBA00030029};
GN   Name=FTCD {ECO:0000313|Ensembl:ENSOANP00000021398.2};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000021398.2, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000021398.2, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021398.2,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000021398.2}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021398.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Binds and promotes bundling of vimentin filaments originating
CC       from the Golgi. {ECO:0000256|ARBA:ARBA00002680}.
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:0000256|ARBA:ARBA00025506}.
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:0000256|ARBA:ARBA00005082}.
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:0000256|ARBA:ARBA00025915}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Golgi
CC       apparatus {ECO:0000256|ARBA:ARBA00004555}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cyclodeaminase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00010825}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       formiminotransferase family. {ECO:0000256|ARBA:ARBA00008297}.
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DR   AlphaFoldDB; F7DDZ6; -.
DR   STRING; 9258.ENSOANP00000021398; -.
DR   Ensembl; ENSOANT00000021401.3; ENSOANP00000021398.2; ENSOANG00000013566.3.
DR   eggNOG; ENOG502QQBY; Eukaryota.
DR   GeneTree; ENSGT00390000005581; -.
DR   HOGENOM; CLU_040037_1_0_1; -.
DR   InParanoid; F7DDZ6; -.
DR   OMA; GWYIDEY; -.
DR   OrthoDB; 5388914at2759; -.
DR   TreeFam; TF333892; -.
DR   UniPathway; UPA00379; UER00555.
DR   Proteomes; UP000002279; Chromosome 7.
DR   Bgee; ENSOANG00000013566; Expressed in liver and 1 other cell type or tissue.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IEA:Ensembl.
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:0008017; F:microtubule binding; IEA:Ensembl.
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; 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   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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Folate-binding {ECO:0000256|ARBA:ARBA00022954};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..180
FT                   /note="Formiminotransferase N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01222"
FT   DOMAIN          181..325
FT                   /note="Formiminotransferase C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01221"
SQ   SEQUENCE   541 AA;  59373 MW;  B4CAECBC2EB4AD43 CRC64;
     MSRLVECVPN FSEGNKKEVI DAIAKAISQT QGCALLDVDA GPSTNRTVYT FVGTPEDVVQ
     GALNAARVAF RLIDMTQHRG EHPRMGALDV CPFIPVKNVT MEECITCAHL FGHQLSTELG
     VPVYLYGEAA QKDNRKALPT IRAGEYEGLP EKLRLAEWAP DFGPGSFIPT WGATATGARK
     FLIAFNINLL CTKEQAHRIA LNVREQGRGK DQPGRLKKVQ GIGWYLDEEN IAQVSTNLLD
     FEVTAIHTVY EEICKDAQEL NLPVVGSQLV GLIPLKAILD AAEFYSKKEN LFVLEEEHKI
     RLVVNRLGLD SLSSFNPKER IIEYMVQDGK TDGELISKSL SAFVRQVGAR SAAPGGGSVS
     AAVSAMGAAL GSMVGLMTYG KRQFEDLDPV MRKLIPPFHQ TMNELIVMVD SDSDAFGSYM
     EAMKMPKYTP EEKEQRAAAI QRGLKKAVSV PLSLAEKVNA LWPTLKEMAL YGNLACKSDL
     QVAAKALETG VFGAYCNVLI NLKDVTDEQF KTQIREKVSS LLEEAQQSMT LVLDSLDKRG
     E
//
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