ID G1KD94_ANOCA Unreviewed; 541 AA.
AC G1KD94;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:ENSACAP00000004762.2};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000004762.2, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000004762.2, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000004762.2,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000004762.2}
RP IDENTIFICATION.
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 RefSeq; XP_003215264.1; XM_003215216.3.
DR AlphaFoldDB; G1KD94; -.
DR STRING; 28377.ENSACAP00000004762; -.
DR Ensembl; ENSACAT00000004870.4; ENSACAP00000004762.2; ENSACAG00000004847.4.
DR GeneID; 100558718; -.
DR KEGG; acs:100558718; -.
DR CTD; 10841; -.
DR eggNOG; ENOG502QQBY; Eukaryota.
DR GeneTree; ENSGT00390000005581; -.
DR HOGENOM; CLU_040037_1_0_1; -.
DR OMA; GWYIDEY; -.
DR OrthoDB; 5388914at2759; -.
DR TreeFam; TF333892; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000004847; Expressed in liver and 4 other cell types or tissues.
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:UP000001646};
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; 59823 MW; 7C70181FB6AD953A CRC64;
MSKLVECVPN FSEGNNKAVI DEIGKAISQT EGCVLLDVDA GPSTNRTVYT FVGSPEDAIE
GALNAARRAF ELIDMAKHTG EHPRMGALDV CPFVPVKNVT MEECIHCANL FGKRLADELS
VPVYLYGKAA RKESRRSLPA IRAGEYEALA EKLQKVEWTP DFGPTSFVPR WGATVTGART
FLIAYNINLL CTKELAHRIA LNIREQGRAK DQPGRLKQVQ GMGWYLDEEN IAQVSTNLLD
FETTPLHVVY EEVCKDAKDL NLPVVGSQLV GLIPKKAMLD AAEFYIKKDN LFILEEDHKI
RLVINRLGLD SLSPFNPKER IIEYMVEDNR ESGSLMSLPL YTFVEKVGAR SATPGGGSVS
AAMASLGAAL GLMVGLMTYG KRQFEELDPV MRKLIPPFHQ AMKELVVMVD TDASAFSGYM
AAMKLPKTTP EEKERRTAAM QLGLKNAVGV PFSLAEKVHS LWPFLREMAQ YGNLACKSDI
QVAAKALEAG VFGAYFNVVT NLKDITDEGF KKQMQEKVSH FLEESKKSSA FVLGQLEKRK
M
//
