GenomeNet

Database: UniProt
Entry: K4FTP1_CALMI
LinkDB: K4FTP1_CALMI
Original site: K4FTP1_CALMI 
ID   K4FTP1_CALMI            Unreviewed;       546 AA.
AC   K4FTP1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   13-SEP-2023, entry version 26.
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};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFK11170.1};
RN   [1] {ECO:0000313|EMBL:AFK11170.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:AFK11170.1};
RX   PubMed=23056606;
RA   Tan Y.Y., Kodzius R., Tay B.H., Tay A., Brenner S., Venkatesh B.;
RT   "Sequencing and Analysis of Full-Length cDNAs, 5'-ESTs and 3'-ESTs from a
RT   Cartilaginous Fish, the Elephant Shark (Callorhinchus milii).";
RL   PLoS ONE 7:E47174-E47174(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JX052942; AFK11170.1; -; mRNA.
DR   AlphaFoldDB; K4FTP1; -.
DR   UniPathway; UPA00379; UER00555.
DR   GO; GO:0005814; C:centriole; 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; IEA:UniProtKB-EC.
DR   GO; GO:0030409; F:glutamate formimidoyltransferase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFK11170.1}.
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   546 AA;  59443 MW;  F0A755AFFE28EA79 CRC64;
     MSKLVECVPN FSNGRSKEII DAIAQAIAQS DGCFLLDVDP GPSTNRTVYT FVGSPAAVVE
     GALNAAREAH RLINMATHSG EHPRLGALDV CPFVPVRDVT MEECVQCAVS FGQQLASQLL
     VPVYLYGEAA RHQHRRTLPS IRAGEYEGLQ EKLCDAQWKP DFGPVEFVPS WGATVTGART
     FLIAFNINLL STREQAHRLA LNIREQGRGP GQPGRLLKVQ VMGWYLEEED IAQVSTNLMD
     FKVTGLHNVY EEIRRDAKEL KMPVIGSQLV GLVPLAAMLH TAQYYITRDK LFILTEEQKL
     RLVVSRLGLN LLAPFNVKER IIEYMVPGQE EAGLASLSLT GFVRSVGART AAPGGGSVAA
     AVAAMGAALG SMVGLMSYGK RQFEVVDAVM RRVIPPLHHT AHQLLTMVDT DSRVFSNYMA
     ALKLPKSTME ERARRNAAVQ AGLKEAVNVP LALAETVTSL WSTLEELATC GNLACTSDLQ
     VAVKALELGV FGAQCNVLTN LRDISDQQFN CQARERISQC LSEAGSCSAR LLAVLAERMK
     ADRPAM
//
DBGET integrated database retrieval system