ID A0A091T8S0_NESNO Unreviewed; 542 AA.
AC A0A091T8S0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 27.
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 ORFNames=N333_00672 {ECO:0000313|EMBL:KFQ54538.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ54538.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ54538.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ54538.1};
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; KK946160; KFQ54538.1; -; Genomic_DNA.
DR RefSeq; XP_010018258.1; XM_010019956.1.
DR AlphaFoldDB; A0A091T8S0; -.
DR GeneID; 104409926; -.
DR KEGG; nnt:104409926; -.
DR CTD; 10841; -.
DR OrthoDB; 5388914at2759; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000053840; 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:UP000053840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFQ54538.1}.
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 542 AA; 58811 MW; 7BE7019200F67191 CRC64;
MAKLVECVPN FSEGNNKEVI DALGQAISCT PGCVLLDVDA GASTNRTVYT FVGTPEAVVE
GALSAARVAR QLIDMSRHKG EHPRMGALDV CPFVPVMNVS MEECITCAHV FGQRLAAELG
VPVYLYGEAA QEKSRKALPT IRAGEYEALP EKLAKPEWAP DFGPPTFVSR WGATVTGART
FLIAYNINLL CTKELAHRIA LNIREQGRGT EQPGRLKKVQ GIGWYLEEEN IAQVSTNLLD
FETTPLHAIY EEVCRDAKAL NLPVVGSQLV GLVPKKALLD AAEFYMKKEN LFILEEEQKI
RLVVSRLGLD SLAPFHPRER IIEYLVQVGE AGDGGLVAKP LGAFVRAVGG RSAAPGGGSV
SAAVGALGAA LGCMVGLMSY GKRQFEALDP IMRKLIPTFH QAMDELVVMV DADSRAFSSY
MEALKLPKST PEEQERRMAA MQEGLKTAVR VPCALAEKVS GLWPALKELA RHCNLACKSD
IQVGVKMLEA AVFGAYFNVM INLKDITDEE FKLAMSQKVS ALLEEAKQGS ALILVLLEKR
VA
//
