ID U2P6T8_9BACT Unreviewed; 567 AA.
AC U2P6T8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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|EMBL:ERK39871.1};
GN ORFNames=HMPREF9135_0211 {ECO:0000313|EMBL:ERK39871.1};
OS Segatella baroniae F0067.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK39871.1, ECO:0000313|Proteomes:UP000016648};
RN [1] {ECO:0000313|EMBL:ERK39871.1, ECO:0000313|Proteomes:UP000016648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0067 {ECO:0000313|EMBL:ERK39871.1,
RC ECO:0000313|Proteomes:UP000016648};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERK39871.1}.
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DR EMBL; AWEY01000008; ERK39871.1; -; Genomic_DNA.
DR RefSeq; WP_021589000.1; NZ_AWEY01000008.1.
DR AlphaFoldDB; U2P6T8; -.
DR PATRIC; fig|1115809.3.peg.686; -.
DR UniPathway; UPA00379; UER00555.
DR Proteomes; UP000016648; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UP000016648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERK39871.1}.
FT DOMAIN 6..186
FT /note="Formiminotransferase N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01222"
FT DOMAIN 187..352
FT /note="Formiminotransferase C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01221"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61377 MW; 4A4503EA218D83B5 CRC64;
MVQEKQIIEC VPNFSEGRNK EVIKQITDEV ECVKGVKLLD VDPGEATNRT VVTFVGEPQV
VVEAAFRCVK KAAQLIDMRQ HHGAHPRMGA TDVCPLIPVA GITLEECARL ARQLAERIAA
ELKVPCYCYE AAAATPERKN LAVCRKGEYE GLPERMTSPA DAPDYGARAW DEQLARTGCT
AVGARDFLIA TNFNLNTTST RRANAIAFDV REKGRPQREG GSPVGKPMKD ADGKTIMIPG
TLKSTKAIGW FIDEYGIAQV SMNITDINVT PLHVAFDEVC RCAQNRGIRV TGTEIVGLIP
KRTLIEAGRY FLKKQNRSTG IPEEDILKIA IKSMGLDDLK PFNPREKVIE YLLEDAHKSK
KLIDLTVKGF ADETSRESPA PGGGTISAYM GALGAALGTM VANLSSHKAG WDDRWEEFST
WAERGQAIQA ELMTLVDEDT EAFNRIMAAF GLPKGTDEEK AARMVAIQEA TLFATEVPLH
TMQASIKVFE LCRAMAEEGN PNSVSDAGVG VLAARAAVLG AGLNVKINAG GLKDRAAADR
LVGQANALIA QANTAEAEIM KIVEAKL
//
