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Database: UniProt
Entry: A0A091IW18_EGRGA
LinkDB: A0A091IW18_EGRGA
Original site: A0A091IW18_EGRGA 
ID   A0A091IW18_EGRGA        Unreviewed;       539 AA.
AC   A0A091IW18;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 22.
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};
DE   Flags: Fragment;
GN   ORFNames=Z169_14951 {ECO:0000313|EMBL:KFP12502.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP12502.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP12502.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP12502.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK501092; KFP12502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IW18; -.
DR   STRING; 188379.A0A091IW18; -.
DR   UniPathway; UPA00379; UER00555.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
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   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:UP000053119};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFP12502.1}.
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"
FT   NON_TER         539
FT                   /evidence="ECO:0000313|EMBL:KFP12502.1"
SQ   SEQUENCE   539 AA;  58725 MW;  610DD075007E7B95 CRC64;
     MAKLVECVPN FSEGNNKEVI NALGQAISQT PGCVLLDVDA GASTNRTVYT FVGSPEAVVE
     GALSAARVAG QLIDMSRHTG EHPRMGALDV CPFVPVMNIS MEECVTCAHI FGQRLAAELG
     VPVYLYGEAA REESRKALPA IRAGEYEALP EKLAKPEWAP DFGPPTFVPQ WGATVTGART
     FLIAYNVNLL CTKELAHRIA LNLREQGRST DQPGRLKKVQ GIGWYLEEEN IAQVSTNLLD
     FETTPLHAVY EEVCRDAEAL NLPVVGSQLV GLVPKKAMLD TAEFYIKKEK LFILEEEQKI
     RLVVSRLGLD SLSPFHPRER IIEYLVQAGE VDRGLVAKPL DAFVRAVGGR SAAPGGGSVS
     AAAAALGAAL GCMVGLMSYG KRQFEELDPI MRKLIPPFHQ AMDELVAMVD ADSRAFSSYM
     EAMKLPKSTA EERERRMAAM QQGLKTAVRV PCTLAEKVNG LWPALKELAH HCNLACKSDI
     QVGAKMLEAA VFGAYFNVMI NLKDITDEKF KLAMSQKVSA LLEEAKQGSA LVLELLEKR
//
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